EcoliWiki - User contributions [en]

PMID:3891721

2008-03-19T15:45:54Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Schirch, V, Hopkins, S, Villar, E and Angelaccio, S''' (1985) Serine hydroxymethyltransferase from Escherichia coli: purification and properties.''J. Bacteriol.'' '''163''':1-7

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Serine hydroxymethyltransferase from Escherichia coli was purified to homogeneity. The enzyme was a homodimer of identical subunits with a molecular weight of 95,000. The amino acid sequence of the amino and carboxy-terminal ends and the amino acid composition of cysteine-containing tryptic peptides were in agreement with the primary structure proposed for this enzyme from the structure of the glyA gene (M. Plamann, L. Stauffer, M. Urbanowski, and G. Stauffer, Nucleic Acids Res. 11:2065-2074, 1983). The enzyme contained no disulfide bonds but had one sulfhydryl group on the surface of the protein. Several sulfhydryl reagents reacted with this exposed group and inactivated the enzyme. Spectra of the enzyme in the presence of substrates and substrate analogs showed that the enzyme formed the same complexes and in similar relative concentrations as previously observed with the cytosolic and mitochondrial rabbit liver isoenzymes. Kinetic studies with substrates showed that the affinity and synergistic binding of the amino acid and folate substrates were similar to those obtained with the rabbit liver isoenzymes. The enzyme catalyzed the cleavage of threonine, allothreonine, and 3-phenylserine to glycine and the corresponding aldehyde in the absence of tetrahydrofolate. The enzyme was also inactivated by D-alanine caused by the transamination of the active site pyridoxal phosphate to pyridoxamine phosphate. This substrate specificity was also observed with the rabbit liver isoenzymes. We conclude that the reaction mechanism and the active site structure of E. coli serine hydroxymethyltransferase are very similar to the mechanism and structure of the rabbit liver isoenzymes.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3891721 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='238161'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Serine Hydroxymethyltransferase
|

|
GO:0004372
|
glycine hydroxymethyltransferase activity
|
IDA: Inferred from Direct Assay
|

|
F
|
See Table 1.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.X47ab4aa1263d6&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

glyA:Gene Product(s)

2008-03-19T15:44:28Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|glyA}}{{Tab|Gene|glyA}}{{Tab On|Gene Product(s)|glyA}}{{Tab|Expression|glyA}}{{Tab|Evolution|glyA}}{{Tab|On One Page|glyA}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
GlyA product
|-
!{{table heading style}} |Synonyms
|
serine hydroxymethyltransferase product<ref name='LIB:Riley_2006'/>, B2551 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, GlyA product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
GlyA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:glycine hydroxymethyltransferase|glycine hydroxymethyltransferase]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.P46aaaf0042cfc&page=25388&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='170210'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009063
|
amino acid catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006545
|
glycine biosynthetic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0046656
|
folic acid biosynthetic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009257
|
10-formyltetrahydrofolate biosynthetic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0004372
|
glycine hydroxymethyltransferase activity
|
[[PMID:6190704]]<ref name=PMID:6190704/>
|
IMP: Inferred from Mutant Phenotype
|

|
F
|

|
complete
|-
|

|
GO:0004372
|
glycine hydroxymethyltransferase activity
|
[[PMID:3891721]]<ref name=PMID:3891721/>
|
IDA: Inferred from Direct Assay
|

|
F
|

|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.P46aaaf01acdec&page=25388&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='170211'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:glycine hydroxymethyltransferase|glycine hydroxymethyltransferase]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.V46aaaf28b2a13&page=25388&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='115453'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.L46a8477e99b2b&page=25388&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=GLYOHMETRANS-MONOMER at EcoCyc]
<pre>MLKREMNIAD YDAELWQAME QEKVRQEEHI ELIASENYTS PRVMQAQGSQ LTNKYAEGYP
GKRYYGGCEY VDIVEQLAID RAKELFGADY ANVQPHSGSQ ANFAVYTALL EPGDTVLGMN
LAHGGHLTHG SPVNFSGKLY NIVPYGIDAT GHIDYADLEK QAKEHKPKMI IGGFSAYSGV
VDWAKMREIA DSIGAYLFVD MAHVAGLVAA GVYPNPVPHA HVVTTTTHKT LAGPRGGLIL
AKGGSEELYK KLNSAVFPGG QGGPLMHVIA GKAVALKEAM EPEFKTYQQQ VAKNAKAMVE
VFLERGYKVV SGGTDNHLFL VDLVDKNLTG KEADAALGRA NITVNKNSVP NDPKSPFVTS
GIRVGTPAIT RRGFKEAEAK ELAGWMCDVL DSINDEAVIE RIKGKVLDIC ARYPVYA</pre>
|-
!{{table heading style}} |Mol. Wt
|
45.32 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|
6.41<ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |Extinction coefficient
|
46300 - 46675 (calc based on 20 Y, 3 W, and 3 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.K46aaaf2b167c2&page=25388&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='170213'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.P46aaaf2b8a140&page=25388&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='170214'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1EQB 1EQB] X-RAY CRYSTAL STRUCTURE AT 2.7 ANGSTROMS RESOLUTION OF TERNARY COMPLEX BETWEEN THE Y65F MUTANT OF E-COLI SERINE HYDROXYMETHYLTRANSFERASE, GLYCINE AND 5-FORMYL TETRAHYDROFOLATE
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.M46aaaf2be7875&page=25388&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='170215'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.R46aaaf2ccdf08&page=25388&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='170216'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=GLYOHMETRANS-MONOMER EcoCyc:GLYOHMETRANS-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0A825 UniProt:P0A825]
|

|-
|
[http://pfam.sanger.ac.uk/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://pfam.sanger.ac.uk/family?acc=PF00464 PFAM:PF00464]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_417046 RefSeq:NP_417046]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P0A825 ModBase:P0A825]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1EQB PDB:1EQB]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.J46aaaf2d3888b&page=25388&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='115454'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.Y46a847850b469&page=25388&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0009063_!_amino acid catabolic process]][[Category:GO:0006545_!_glycine biosynthetic process]][[Category:GO:0046656_!_folic acid biosynthetic process]][[Category:GO:0009257_!_10-formyltetrahydrofolate biosynthetic process]][[Category:Complex:glycine hydroxymethyltransferase]][[Category:Products with structures in PDB]]

PMID:6190704

2008-03-19T15:41:13Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Plamann, MD and Stauffer, GV''' (1983) Characterization of the Escherichia coli gene for serine hydroxymethyltransferase.''Gene'' '''22''':9-18

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Plasmid pGS1 carries the Escherichia coli glyA gene and its neighboring regions on a 13-kb EcoRI insert. In a cell-free transcription-translation system, the insert directs the synthesis of two polypeptides with Mr values of about 46 500 and 45 500. When the glyA gene is inactivated with the transposable element Tn5, the Mr 46 500 polypeptide is not observed, identifying it as the glyA gene product. The Mr 45 500 polypeptide is the product of an unknown gene designated gene X. When plasmids with random insertions of the Tn5 element in either the glyA gene or gene X are used as templates in the cell-free transcription-translation system, the polypeptides observed are smaller than the glyA or X gene products. A comparison of the site of each Tn5 insertion within the glyA gene or within gene X and the size of the polypeptide observed in the cell-free system enabled us to determine the direction of transcription and translation of both genes. The glyA gene is transcribed and translated in a direction opposite to that of gene X. Nucleotide sequencing confirmed the location and orientation of the two genes in the insert. DNase I footprinting experiments defined the glyA gene and gene X control regions recognized by RNA polymerase, and S1 nuclease mapping experiments located the transcription start point for each gene. The transcription start points for the two genes are 216 bp apart, and the translation start sites are 327 bp apart. Less than 90 bp separate the two RNA polymerase molecules bound to the two promoters.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6190704 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241530'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Serine Hydroxymethyltransferase
|

|
GO:0004372
|
glycine hydroxymethyltransferase activity
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
See Fig. 1 and Results section (a).
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.U47e1339f59086&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:6190704

2008-03-19T15:39:11Z

Michelle: New PMID: Page!

<protect>
{{RightTOC}}

 '''Plamann, MD and Stauffer, GV''' (1983) Characterization of the Escherichia coli gene for serine hydroxymethyltransferase.''Gene'' '''22''':9-18

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Plasmid pGS1 carries the Escherichia coli glyA gene and its neighboring regions on a 13-kb EcoRI insert. In a cell-free transcription-translation system, the insert directs the synthesis of two polypeptides with Mr values of about 46 500 and 45 500. When the glyA gene is inactivated with the transposable element Tn5, the Mr 46 500 polypeptide is not observed, identifying it as the glyA gene product. The Mr 45 500 polypeptide is the product of an unknown gene designated gene X. When plasmids with random insertions of the Tn5 element in either the glyA gene or gene X are used as templates in the cell-free transcription-translation system, the polypeptides observed are smaller than the glyA or X gene products. A comparison of the site of each Tn5 insertion within the glyA gene or within gene X and the size of the polypeptide observed in the cell-free system enabled us to determine the direction of transcription and translation of both genes. The glyA gene is transcribed and translated in a direction opposite to that of gene X. Nucleotide sequencing confirmed the location and orientation of the two genes in the insert. DNase I footprinting experiments defined the glyA gene and gene X control regions recognized by RNA polymerase, and S1 nuclease mapping experiments located the transcription start point for each gene. The transcription start points for the two genes are 216 bp apart, and the translation start sites are 327 bp apart. Less than 90 bp separate the two RNA polymerase molecules bound to the two promoters.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6190704 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='241530'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.U47e1339f59086&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

glyA:Gene Product(s)

2008-03-19T15:39:01Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|glyA}}{{Tab|Gene|glyA}}{{Tab On|Gene Product(s)|glyA}}{{Tab|Expression|glyA}}{{Tab|Evolution|glyA}}{{Tab|On One Page|glyA}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
GlyA product
|-
!{{table heading style}} |Synonyms
|
serine hydroxymethyltransferase product<ref name='LIB:Riley_2006'/>, B2551 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, GlyA product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
GlyA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:glycine hydroxymethyltransferase|glycine hydroxymethyltransferase]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.P46aaaf0042cfc&page=25388&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='170210'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009063
|
amino acid catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006545
|
glycine biosynthetic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0046656
|
folic acid biosynthetic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009257
|
10-formyltetrahydrofolate biosynthetic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0004372
|
glycine hydroxymethyltransferase activity
|
[[PMID:6190704]]<ref name=PMID:6190704/>
|
IMP: Inferred from Mutant Phenotype
|

|
F
|

|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.P46aaaf01acdec&page=25388&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='170211'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:glycine hydroxymethyltransferase|glycine hydroxymethyltransferase]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.V46aaaf28b2a13&page=25388&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='115453'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.L46a8477e99b2b&page=25388&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=GLYOHMETRANS-MONOMER at EcoCyc]
<pre>MLKREMNIAD YDAELWQAME QEKVRQEEHI ELIASENYTS PRVMQAQGSQ LTNKYAEGYP
GKRYYGGCEY VDIVEQLAID RAKELFGADY ANVQPHSGSQ ANFAVYTALL EPGDTVLGMN
LAHGGHLTHG SPVNFSGKLY NIVPYGIDAT GHIDYADLEK QAKEHKPKMI IGGFSAYSGV
VDWAKMREIA DSIGAYLFVD MAHVAGLVAA GVYPNPVPHA HVVTTTTHKT LAGPRGGLIL
AKGGSEELYK KLNSAVFPGG QGGPLMHVIA GKAVALKEAM EPEFKTYQQQ VAKNAKAMVE
VFLERGYKVV SGGTDNHLFL VDLVDKNLTG KEADAALGRA NITVNKNSVP NDPKSPFVTS
GIRVGTPAIT RRGFKEAEAK ELAGWMCDVL DSINDEAVIE RIKGKVLDIC ARYPVYA</pre>
|-
!{{table heading style}} |Mol. Wt
|
45.32 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|
6.41<ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |Extinction coefficient
|
46300 - 46675 (calc based on 20 Y, 3 W, and 3 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.K46aaaf2b167c2&page=25388&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='170213'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.P46aaaf2b8a140&page=25388&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='170214'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1EQB 1EQB] X-RAY CRYSTAL STRUCTURE AT 2.7 ANGSTROMS RESOLUTION OF TERNARY COMPLEX BETWEEN THE Y65F MUTANT OF E-COLI SERINE HYDROXYMETHYLTRANSFERASE, GLYCINE AND 5-FORMYL TETRAHYDROFOLATE
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.M46aaaf2be7875&page=25388&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='170215'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.R46aaaf2ccdf08&page=25388&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='170216'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=GLYOHMETRANS-MONOMER EcoCyc:GLYOHMETRANS-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0A825 UniProt:P0A825]
|

|-
|
[http://pfam.sanger.ac.uk/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://pfam.sanger.ac.uk/family?acc=PF00464 PFAM:PF00464]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_417046 RefSeq:NP_417046]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P0A825 ModBase:P0A825]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1EQB PDB:1EQB]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.J46aaaf2d3888b&page=25388&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='115454'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25388.Y46a847850b469&page=25388&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0009063_!_amino acid catabolic process]][[Category:GO:0006545_!_glycine biosynthetic process]][[Category:GO:0046656_!_folic acid biosynthetic process]][[Category:GO:0009257_!_10-formyltetrahydrofolate biosynthetic process]][[Category:Complex:glycine hydroxymethyltransferase]][[Category:Products with structures in PDB]]

PMID:6102982

2008-03-19T15:14:39Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Humbert, R and Simoni, RD''' (1980) Genetic and biomedical studies demonstrating a second gene coding for asparagine synthetase in Escherichia coli.''J. Bacteriol.'' '''142''':212-20

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Genetic experiments have indicated that asparagine auxotrophs of Escherichias coli K-12 can be made asparagine prototrophs at either of two sites on the chromosome and that wild-type strains require both sites to be mutated to produce asparagine auxotrophy. The former asn locus is now called asnA, and the new gene is designated asnB. The asnB gene is located near gal.AsnA+ asnB and asnA asnB+ strains were constructed, and the asparagine synthetic reaction was characterized in extracts. These studies revealed that the asnA gene codes for the enzyme previously described (H. Cedar and J.H. Schwartz, J. Biol. Chem. 244: 4112-4121, 1969), whereas the asnB gene is involved in the production of an enzyme which differs from the one previously described in its specific activity in extracts, its stability at low and high temperatures, and its apparent ability to use either glutamine or ammonia as amide nitrogen donor. Physiological studies showed that either enzyme alone is sufficient to allow a maximal growth rate under conditions of asparagine limitation.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6102982 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221982'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Asparaginase
|

|
GO:0004067
|
asparaginase activity
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
See Table 3.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.J47a144d25dae9&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

asnB:Gene Product(s)

2008-03-19T15:11:43Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|asnB}}{{Tab|Gene|asnB}}{{Tab On|Gene Product(s)|asnB}}{{Tab|Expression|asnB}}{{Tab|Evolution|asnB}}{{Tab|On One Page|asnB}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
AsnB product
|-
!{{table heading style}} |Synonyms
|
asparagine synthetase B product<ref name='LIB:Riley_2006'/>, B0674 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, AsnB product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
AsnB<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:asparagine synthetase B|asparagine synthetase B]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.4 6.3.5.4]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21080.C46aa3c61ced9d&page=21080&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='156265'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009063
|
amino acid catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006529
|
asparagine biosynthetic process
|
[[PMID:6102982]]<ref name=PMID:6102982/>
|
IMP: Inferred from Mutant Phenotype
|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
complete
|-
|

|
GO:0004067
|
asparaginase activity
|
[[PMID:6102982]]<ref name=PMID:6102982/>
|
IMP: Inferred from Mutant Phenotype
|

|
F
|

|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21080.L46aa3c634559c&page=21080&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='156266'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:asparagine synthetase B|asparagine synthetase B]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21080.F46aa3c75a9f8e&page=21080&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='105244'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21080.K46a7ce1911e6d&page=21080&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=ASNSYNB-MONOMER at EcoCyc]
<pre>MCSIFGVFDI KTDAVELRKK ALELSRLMRH RGPDWSGIYA SDNAILAHER LSIVDVNAGA
QPLYNQQKTH VLAVNGEIYN HQALRAEYGD RYQFQTGSDC EVILALYQEK GPEFLDDLQG
MFAFALYDSE KDAYLIGRDH LGIIPLYMGY DEHGQLYVAS EMKALVPVCR TIKEFPAGSY
LWSQDGEIRS YYHRDWFDYD AVKDNVTDKN ELRQALEDSV KSHLMSDVPY GVLLSGGLDS
SIISAITKKY AARRVEDQER SEAWWPQLHS FAVGLPGSPD LKAAQEVANH LGTVHHEIHF
TVQEGLDAIR DVIYHIETYD VTTIRASTPM YLMSRKIKAM GIKMVLSGEG SDEVFGGYLY
FHKAPNAKEL HEETVRKLLA LHMYDCARAN KAMSAWGVEA RVPFLDKKFL DVAMRINPQD
KMCGNGKMEK HILRECFEAY LPASVAWRQK EQFSDGVGYS WIDTLKEVAA QQVSDQQLET
ARFRFPYNTP TSKEAYLYRE IFEELFPLPS AAECVPGGPS VACSSAKAIE WDEAFKKMDD
PSGRAVGVHQ SAYK</pre>
|-
!{{table heading style}} |Mol. Wt
|
62.66 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
92710 - 93710 (calc based on 29 Y, 9 W, and 8 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21080.A46aa3c77c3e8e&page=21080&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='156268'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21080.L46aa3c782a10b&page=21080&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='156269'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1CT9 1CT9] CRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLI
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21080.Z46aa3c787496c&page=21080&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='156270'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21080.G46aa3c79332c8&page=21080&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='156271'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=ASNSYNB-MONOMER EcoCyc:ASNSYNB-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P22106 UniProt:P22106]
|

|-
|
[http://pfam.sanger.ac.uk/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://pfam.sanger.ac.uk/family?acc=PF00310 PFAM:PF00310]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_415200 RefSeq:NP_415200]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P22106 ModBase:P22106]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1CT9 PDB:1CT9]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21080.Q46aa3c797e887&page=21080&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='105247'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21080.N46a7ce1f3e955&page=21080&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0009063_!_amino acid catabolic process]][[Category:GO:0006529_!_asparagine biosynthetic process]][[Category:Complex:asparagine synthetase B]][[Category:Products with structures in PDB]]

PMID:16562136

2007-11-26T18:08:38Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Böck, A and Neidhardt, FC''' (1966) Isolation of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase Activity.''J Bacteriol'' '''92''':464-469

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Böck, August (Purdue University, Lafayette, Ind.), and Frederick C. Neidhardt. Isolation of a mutant of Escherichia coli with a temperature-sensitive fructose-1,6-diphosphate aldolase activity. J. Bacteriol. 92:464-469. 1966.-A mutant of Escherichia coli was isolated which was able to grow in rich medium at 30 C but not at 40 C. Upon exposure to 40 C, the cells immediately stopped ribonucleic acid (RNA) and deoxyribonucleic acid synthesis, but protein synthesis continued at a diminished rate for a short time. Addition of chloramphenicol did not release RNA synthesis from inhibition at 40 C. Synthesis of beta-galactosidase could be induced at high temperature despite the presence of glucose in the medium, indicating a lesion in glucose catabolism. Of many catabolic enzymes tested in cell-free extracts, only fructose-1,6-diphosphate aldolase activity appeared to be altered in the mutant cells. No activity was demonstrable in extracts of mutant cells grown at either 30 or 40 C, but determination of glucose-oxidation patterns revealed that the enzyme is probably active in vivo at 30 C. Temperature-resistant secondary mutants were found to have partially or fully restored aldolase activity, and temperature-resistant recombinants had normal aldolase activity, indicating that the growth pattern and the altered aldolase had a common genetic basis. Linkage data permitted the assignment of an approximate map location for the mutated aldolase gene.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16562136 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='220849'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
fbaA product: Fructose-bisphosphate aldolase
|

|
GO:0004332
|
fructose-bisphosphate aldolase activity
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
See Table 2.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.R470a5b7417d89&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:4942326

2007-11-26T18:04:38Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Spring, TG and Wold, F''' (1971) The purification and characterization of Escherichia coli enolase.''J. Biol. Chem.'' '''246''':6797-802

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || No abstract in PubMed - copied from pdf:
Enolase has been purified from aqueous extracts of Escherichia coli acetone powder by (a) heat treatment, (b) fractionation with acetone, (c) TEAE-cellulose chromatography, (d) Sephadex G-100 chromatography, and (e) crystallization. The purified, crystalline enzyme migrates as a single band in disc gel electrophoresis and is homogeneous by ultracentrifugal analysis. The molecular weight of the enzyme is approximately 90,000, as determined by sedimentation velocity and sedimentation equilibrium experiments. The subunit molecular weight estimated by electrophoresis in polyacrylamide gels containing sodium dodecyl sulfate is 46,000, suggesting that the enzyme is composed of two subunits of equal size. Functionally there are many similarities between E. coli enolase and other enolases studied. Thus, the dependence on Mg2+ for activity and the inhibition by fluoride in the presence of phosphate are quantitatively very similar for all enolases. Other catalytic parameters (I&, V IllS.X, and pH optimum) are also similar, but minor quantitative distinction indicates that E. coli enolase is more closely related to yeast enolase than to enolases from vertebrate muscle.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4942326 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='220729'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
[[eno]]
|

|
GO:0004634
|
phosphopyruvate hydratase activity
|
IDA: Inferred from Direct Assay
|

|
F
|
See Table 1.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.D46fa87ba30770&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:7592346

2007-11-26T18:02:13Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Sprenger, GA, Schörken, U, Sprenger, G and Sahm, H''' (1995) Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains.''J. Bacteriol.'' '''177''':5930-6

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || A previously recognized open reading frame (T. Yura, H. Mori, H. Nagai, T. Nagata, A. Ishihama, N. Fujita, K. Isono, K. Mizobuchi, and A. Nakata, Nucleic Acids Res. 20:3305-3308) from the 0.2-min region of the Escherichia coli K-12 chromosome is shown to encode a functional transaldolase activity. After cloning of the gene onto high-copy-number vectors, transaldolase B (D-sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate dihydroxyacetone transferase; EC 2.2.1.2) was overexpressed up to 12.7 U mg of protein-1 compared with less than 0.1 U mg of protein-1 in wild-type homogenates. The enzyme was purified from recombinant E. coli K-12 cells by successive ammonium sulfate precipitations (45 to 80% and subsequently 55 to 70%) and two anion-exchange chromatography steps (Q-Sepharose FF, Fractogel EMD-DEAE tentacle column; yield, 130 mg of protein from 12 g of cell wet weight) and afforded an apparently homogeneous protein band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis with a subunit size of 35,000 +/- 1,000 Da. As the enzyme had a molecular mass of 70,000 Da by gel filtration, transaldolase B is likely to form a homodimer. N-terminal amino acid sequencing of the protein verified its identity with the product of the cloned gene talB. The specific activity of the purified enzyme determined at 30 degrees C with the substrates fructose-6-phosphate (donor of C3 compound) and erythrose-4-phosphate (acceptor) at an optimal pH (50 mM glycylglycine [pH 8.5]) was 60 U mg-1.Km values for the substrates fructose-6-phosphate and erythrose-4-phosphate were determined at 1,200 and 90 microM, respectively. Kinetic constants for the other two physiological reactants, D,L-glyceraldehyde 3-phosphate (Km, 38 microM; relative activity [V(rel)], 8%) and sedoheptulose-7-phosphate (K(m), 285 microM; V(rel), 5%) were also determined. Fructose acted as a C(3) donor at a high apparent K(m) (>/=M) and with a V(rel) of 12%. The enzyme was inhibited by Tris-HCl, phosphate, or sugars with the L configuration at C(2) (L-glyceraldehyde, D-arabinose-5-phosphate).
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7592346 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='220372'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
TalB product: Transaldolase
|

|
GO:0004801
|
transaldolase activity
|
IDA: Inferred from Direct Assay
|

|
F
|
An IDA evidence code is noted from Table 1. p.5934. As total activity decreases, specific activity increases.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.E46c32e7a96f74&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
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<references/>

PMID:8366047

2007-11-26T18:01:13Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Hove-Jensen, B and Maigaard, M''' (1993) Escherichia coli rpiA gene encoding ribose phosphate isomerase A.''J. Bacteriol.'' '''175''':5628-35

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The rpiA gene encoding ribose phosphate isomerase A was cloned from phage 1A2(471) of the Kohara gene library. Subcloning, restriction, and complementation analyses revealed an 1,800-bp SspI-generated DNA fragment that contained the entire control and coding sequences. This DNA fragment was sequenced and shown to harbor an open reading frame of 219 codons, sufficient to encode a polypeptide with an M(r) of 22,845. The synthesis of the rpiA-encoded polypeptide was detected by analysis of minicells, which established the subunit M(r) as 27,000. The assignment of the correct reading frame was confirmed by amino-terminal analysis of partially purified ribose phosphate isomerase A. Our data indicate that the enzyme is composed of two identical subunits. The 5' end of the rpiA-specified transcript was analyzed by primer extension, which revealed a well-conserved -10 region 34 bp upstream of the presumed translation start codon. Analysis of the 3' end of the transcript by S1 nuclease mapping showed that transcription termination occurred within an adenylate-rich sequence following a guanylate-cytidylate-rich stem-loop structure resembling a rho factor-independent transcription terminator. Host strains harboring the rpiA gene in a multicopy plasmid contained up to 42-fold as much ribose phosphate isomerase A activity as the haploid strain.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8366047 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221880'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Rpi A product: Ribose-5-Phoshpate Isomerase
|

|
GO:0004751
|
ribose-5-phosphate isomerase activity
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
An IMP evidence code is noted from Figure 1. p.5631 and review of part B which indicates the phenotype that each plasmid confers to an rpiA mutant strain after transformation.
|
complete
|-
|
RpiA product: Ribose-5-Phosphate Isomerase
|

|
GO:0004751
|
ribose-5-phosphate isomerase activity
|
IDA: Inferred from Direct Assay
|

|
F
|
An IDA evidence code is noted from Table 2. p.5632. Table 2 gives the specific activities of rpi ascribed to rpiA because the cells were grown under conditions in which there is virtually no rpiB activity present.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.K473b67dd37cb6&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
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{{RefHelp}}
<references/>

PMID:4945194

2007-11-26T17:58:36Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Fradkin, JE and Fraenkel, DG''' (1971) 2-keto-3-deoxygluconate 6-phosphate aldolase mutants of Escherichia coli.''J. Bacteriol.'' '''108''':1277-83

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || A new mutation in Escherichia coli, giving inability to grow on gluconic, glucuronic, or galacturonic acids, has been identified as complete deficiency of 2-keto-3-deoxygluconate 6-phosphate (KDGP) aldolase activity. The genetic map position of the locus, eda, is about 35 min. The inability to grow on the uronic acids was expected, because the aldolase is on the sole known pathway of their metabolism. However, inability to grow on gluconate was less expected, because the hexose monophosphate shunt might be used, as happens in mutants blocked in the previous step, edd, of the Entner-Doudoroff pathway. The likely explanation of gluconate negativity is inhibition by accumulated KDGP, because gluconate is inhibitory to growth on other substances, and one type of gluconate revertant is eda(-), edd(-). KDGP is probably the inducer of KDGP aldolase.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4945194 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221646'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
KDPG
|

|
GO:0008675
|
2-dehydro-3-deoxy-phosphogluconate aldolase activity
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
An IMP evidence code is noted from Table 1. p.1279 due to absence of activity in mutant.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.P4728ed4f78545&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
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{{RefHelp}}
<references/>

PMID:5337844

2007-11-26T17:56:33Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Zablotny, R and Fraenkel, DG''' (1967) Glucose and gluconate metabolism in a mutant of Escherichia coli lacking gluconate-6-phosphate dehydrase.''J. Bacteriol.'' '''93''':1579-81

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || A mutant lacking gluconate-6-phosphate dehydrase (the first enzyme of the Entner-Doudoroff pathway) was isolated after ethyl methane sulfonate mutagenesis of Escherichia coli. Other enzymes of gluconate metabolism (gluconokinase, gluconate-6-phosphate dehydrogenase, and 2-keto-3-deoxygluconate-6-phosphate aldolase) were present in the mutant. When the mutant was grown on gluconate-1-(14)C, alanine isolated from protein was unlabeled, showing that the dehydrase was absent in vivo and that the sole pathway of gluconate metabolism in the mutant was the hexose monophosphate shunt. The mutant grew on gluconate with a doubling time of 155 min, compared with the parent strain's 56 min. On glucose and fructose it grew with normal doubling times. Thus, in E. coli, the Entner-Doudoroff pathway is used for gluconate metabolism but not for glucose metabolism.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=5337844 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221645'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
6-Phosphogluconate Dehydratase
|

|
GO:0004456
|
phosphogluconate dehydratase activity
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
See Table 1.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.B4728ed3dc73be&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

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{{RefHelp}}
<references/>

PMID:4942754

2007-11-26T17:53:27Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Adhya, S and Schwartz, M''' (1971) Phosphoglucomutase mutants of Escherichia coli K-12.''J. Bacteriol.'' '''108''':621-6

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Bacteria with strongly depressed phosphoglucomutase (EC 2.7.5.1) activity are found among the mutants of Escherichia coli which, when grown on maltose, accumulate sufficient amylose to be detectable by iodine staining. These pgm mutants grow poorly on galactose but also accumulate amylose on this carbon source. Growth on lactose does not produce high amylose but, instead, results in the induction of the enzymes of maltose metabolism, presumably by accumulation of maltose. These facts suggest that the catabolism of glucose-1-phosphate is strongly depressed in pgm mutants, although not completely abolished. Anabolism of glucose-1-phosphate is also strongly depressed, since amino acid- or glucose-grown pgm mutants are sensitive to phage C21, indicating a deficiency in the biosynthesis of uridine diphosphoglucose or uridine diphosphogalactose, or both. All pgm mutations isolated map at about 16 min on the genetic map, between purE and the gal operon.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4942754 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221123'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Phosphoglucomutase
|

|
GO:0004614
|
phosphoglucomutase activity
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
See Table 1.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.O471bed4e2858a&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:15766779

2007-11-26T17:51:29Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Zimenkov, D, Gulevich, A, Skorokhodova, A, Biriukova, I, Kozlov, Y and Mashko, S''' (2005) Escherichia coli ORF ybhE is pgl gene encoding 6-phosphogluconolactonase (EC 3.1.1.31) that has no homology with known 6PGLs from other organisms.''FEMS Microbiol. Lett.'' '''244''':275-80

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The pentose-phosphate pathway (PPP) is an important part of central metabolism in many organisms. A pgl(-) mutation that decreases the efficiency of the second stage of PPP has been described and mapped at approx. 17.2 min of the Escherichia coli chromosome more than 30 years ago. Although it has recently been shown that deletion of ORF ybhE leads to earlier detected Pgl(-) phenotype for E. coli mutant strain, 6-phosphogluconolactonase from this organism has not been characterized. In the present, independent investigation we show that the Pgl(-) phenotype of DeltaybhE MG1655 could be complemented by insertion of the well-characterized pgl gene from Pseudomonas putida whose protein product has no visible homology with E. coli YbhE. Moreover, a final confirmation that ybhE actually encodes 6PGL in E. coli was obtained through overexpression of the cloned gene, purification of the protein product, followed by direct determination of its enzymatic activity in vitro.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15766779 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221906'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
6-Phosphogluconolactonase
|

|
GO:0017057
|
6-phosphogluconolactonase activity
|
IDA: Inferred from Direct Assay
|

|
F
|
See fourth paragraph of section 3.3.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.T474b073ebbd02&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

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{{RefHelp}}
<references/>

PMID:15766779

2007-11-26T17:49:51Z

Michelle: New PMID: Page!

<protect>
{{RightTOC}}

 '''Zimenkov, D, Gulevich, A, Skorokhodova, A, Biriukova, I, Kozlov, Y and Mashko, S''' (2005) Escherichia coli ORF ybhE is pgl gene encoding 6-phosphogluconolactonase (EC 3.1.1.31) that has no homology with known 6PGLs from other organisms.''FEMS Microbiol. Lett.'' '''244''':275-80

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The pentose-phosphate pathway (PPP) is an important part of central metabolism in many organisms. A pgl(-) mutation that decreases the efficiency of the second stage of PPP has been described and mapped at approx. 17.2 min of the Escherichia coli chromosome more than 30 years ago. Although it has recently been shown that deletion of ORF ybhE leads to earlier detected Pgl(-) phenotype for E. coli mutant strain, 6-phosphogluconolactonase from this organism has not been characterized. In the present, independent investigation we show that the Pgl(-) phenotype of DeltaybhE MG1655 could be complemented by insertion of the well-characterized pgl gene from Pseudomonas putida whose protein product has no visible homology with E. coli YbhE. Moreover, a final confirmation that ybhE actually encodes 6PGL in E. coli was obtained through overexpression of the cloned gene, purification of the protein product, followed by direct determination of its enzymatic activity in vitro.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15766779 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

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<protect>

{|class = 'sortable' {{Prettytable}} id='221906'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.T474b073ebbd02&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
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<references/>

PMID:15576773

2007-11-26T17:49:18Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Thomason, LC, Court, DL, Datta, AR, Khanna, R and Rosner, JL''' (2004) Identification of the Escherichia coli K-12 ybhE gene as pgl, encoding 6-phosphogluconolactonase.''J. Bacteriol.'' '''186''':8248-53

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || We report identification of the Escherichia coli ybhE gene as the pgl gene that encodes 6-phosphogluconolactonase. A tentative identification was first made based on the known approximate location of the pgl gene and the similarity of the presumptive ybhE-encoded protein sequence to a known Pgl enzyme. To test this notion, the ybhE gene was deleted and replaced with a drug marker. Like previously characterized pgl mutants, the ybhE deletion mutant had a Blu- phenotype (dark-blue staining with iodine due to accumulation of starch after growth on minimal maltose) and demonstrated impaired growth on minimal glucose medium when combined with a pgi mutation. Biochemical assay of crude extracts for 6-phosphogluconolactonase enzymatic activity showed that ybhE encodes this activity. The ybhE gene was transferred from the E. coli chromosome to an expression vector. This ybhE clone complemented both the precise deletion of the ybhE gene and a larger deletion, pglDelta8, for the Blu- phenotype and for phosphogluconolactonase activity, confirming that ybhE is the pgl gene. A newly observed phenotype of pgl strains is a lowered frequency of appearance of Bgl+ mutants that can utilize the beta-glucoside salicin. This is likely due to poor growth of Bgl+ pgl strains on salicin due to the accumulation of 6-phosphogluconolactone.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15576773 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

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<protect>

{|class = 'sortable' {{Prettytable}} id='221414'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
6-Phosphogluconolactonase
|

|
GO:0017057
|
6-phosphogluconolactonase activity
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
See Figure 4.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.A47245b13b4baa&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

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{{RefHelp}}
<references/>

PMID:8576032

2007-11-26T17:45:39Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Sørensen, KI and Hove-Jensen, B''' (1996) Ribose catabolism of Escherichia coli: characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression.''J. Bacteriol.'' '''178''':1003-11

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Escherichia coli strains defective in the rpiA gene, encoding ribose phosphate isomerase A, are ribose auxotrophs, despite the presence of the wild-type rpiB gene, which encodes ribose phosphate isomerase B. Ribose prototrophs of an rpiA genetic background were isolated by two different approaches. Firstly, spontaneous ribose-independent mutants were isolated. The locus for this lesion, rpiR, was mapped to 93 min on the linkage map, and the gene order zje::Tn10-rpiR-mel-zjd::Tn10-psd-purA was established. Secondly, ribose prototrophs resulted from the cloning of the rpiB gene on a multicopy plasmid. The rpiB gene resided on a 4.6-kbp HindIII-EcoRV DNA fragment from phage lambda 10H5 (642) of the Kohara gene library and mapped at 92.85 min. Consistent with this map position, the cloned DNA fragment contained two divergent open reading frames of 149 and 296 codons, encoding ribose phosphate isomerase B (molecular mass, 16,063 Da) and a negative regulator of rpiB gene expression, RpiR (molecular mass, 32,341 Da), respectively. The 5' ends of rpiB- and rpiR-specified transcripts were located by primer extension analysis. No significant amino acid sequence similarity was found between ribose phosphate isomerases A and B, but ribose phosphate isomerase B exhibited high-level similarity to both LacA and LacB subunits of the galactose 6-phosphate isomerases of several gram-positive bacteria. Analyses of strains containing rpiA, rpiB, or rpiA rpiB mutations revealed that both enzymes were equally efficient in catalyzing the isomerization step in either direction and that the construction of rpiA rpiB double mutants was a necessity to fully prevent this reaction.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8576032 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221905'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Ribose-5-Phoshpate Isomerase
|

|
GO:0004751
|
ribose-5-phosphate isomerase activity
|
IDA: Inferred from Direct Assay
|

|
F
|
See Table 2.
|
complete
|-
|
Ribose-5-Phosphate Isomerase
|

|
GO:0004751
|
ribose-5-phosphate isomerase activity
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
See Figure 2.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.V474b05e33b691&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:8576032

2007-11-26T17:44:03Z

Michelle: New PMID: Page!

<protect>
{{RightTOC}}

 '''Sørensen, KI and Hove-Jensen, B''' (1996) Ribose catabolism of Escherichia coli: characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression.''J. Bacteriol.'' '''178''':1003-11

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Escherichia coli strains defective in the rpiA gene, encoding ribose phosphate isomerase A, are ribose auxotrophs, despite the presence of the wild-type rpiB gene, which encodes ribose phosphate isomerase B. Ribose prototrophs of an rpiA genetic background were isolated by two different approaches. Firstly, spontaneous ribose-independent mutants were isolated. The locus for this lesion, rpiR, was mapped to 93 min on the linkage map, and the gene order zje::Tn10-rpiR-mel-zjd::Tn10-psd-purA was established. Secondly, ribose prototrophs resulted from the cloning of the rpiB gene on a multicopy plasmid. The rpiB gene resided on a 4.6-kbp HindIII-EcoRV DNA fragment from phage lambda 10H5 (642) of the Kohara gene library and mapped at 92.85 min. Consistent with this map position, the cloned DNA fragment contained two divergent open reading frames of 149 and 296 codons, encoding ribose phosphate isomerase B (molecular mass, 16,063 Da) and a negative regulator of rpiB gene expression, RpiR (molecular mass, 32,341 Da), respectively. The 5' ends of rpiB- and rpiR-specified transcripts were located by primer extension analysis. No significant amino acid sequence similarity was found between ribose phosphate isomerases A and B, but ribose phosphate isomerase B exhibited high-level similarity to both LacA and LacB subunits of the galactose 6-phosphate isomerases of several gram-positive bacteria. Analyses of strains containing rpiA, rpiB, or rpiA rpiB mutations revealed that both enzymes were equally efficient in catalyzing the isomerization step in either direction and that the construction of rpiA rpiB double mutants was a necessity to fully prevent this reaction.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8576032 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221905'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.V474b05e33b691&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

rpiB:Gene Product(s)

2007-11-26T17:43:50Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|alsI}}{{Tab|Gene|alsI}}{{Tab On|Gene Product(s)|alsI}}{{Tab|Expression|alsI}}{{Tab|Evolution|alsI}}{{Tab|On One Page|alsI}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
RpiB product
|-
!{{table heading style}} |Synonyms
|
ribose 5-phosphate isomerase B/allose 6-phosphate isomerase product<ref name='LIB:Riley_2006'/>, B4090 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, YjcA product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, AlsI product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, RpiB product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
AlsI<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:RIB5PISOMB-CPLX|RIB5PISOMB-CPLX]]<ref name='LIB:EcoCyc10.6'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6]<ref name='LIB:Riley_2006'/>
* [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=5.3.1.- 5.3.1.-]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28868.D46ab1c1e2b3fc&page=28868&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='181528'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0016052
|
carbohydrate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009052
|
pentose-phosphate shunt, non-oxidative branch
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0004751
|
ribose-5-phosphate isomerase activity
|
[[PMID:8576032]]<ref name=PMID:8576032/>
|
IDA: Inferred from Direct Assay
|

|
F
|

|
complete
|-
|

|
GO:0004751
|
ribose-5-phosphate isomerase activity
|
[[PMID:8576032]]<ref name=PMID:8576032/>
|
IMP: Inferred from Mutant Phenotype
|

|
F
|

|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28868.Y46ab1c1fb1ceb&page=28868&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='181529'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:RIB5PISOMB-CPLX|RIB5PISOMB-CPLX]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28868.K46ab1c2fe6fb9&page=28868&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='181530'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28868.T46ab1c3142863&page=28868&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=RIB5PISOMB-MONOMER at EcoCyc]
<pre>MKKIAFGCDH VGFILKHEIV AHLVERGVEV IDKGTWSSER TDYPHYASQV ALAVAGGEVD
GGILICGTGV GISIAANKFA GIRAVVCSEP YSAQLSRQHN DTNVLAFGSR VVGLELAKMI
VDAWLGAQYE GGRHQQRVEA ITAIEQRRN</pre>
|-
!{{table heading style}} |Mol. Wt
|
16.07 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
16960 - 17335 (calc based on 4 Y, 2 W, and 3 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28868.V46ab1c328b371&page=28868&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='181532'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28868.J46ab1c330eba2&page=28868&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='181533'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1NN4 1NN4] Structural Genomics, RpiB/AlsB
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28868.F46ab1c33764be&page=28868&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='181534'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28868.P46ab1c3472f70&page=28868&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='181535'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=RIB5PISOMB-MONOMER EcoCyc:RIB5PISOMB-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P37351 UniProt:P37351]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF02502 PFAM:PF02502]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_418514 RefSeq:NP_418514]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P37351 ModBase:P37351]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1NN4 PDB:1NN4]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28868.Y46ab1c34d9bb8&page=28868&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='181536'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28868.D46ab1c396111e&page=28868&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0016052_!_carbohydrate catabolic process]][[Category:GO:0009052_!_pentose-phosphate shunt, non-oxidative branch]][[Category:Complex:RIB5PISOMB-CPLX]][[Category:Products with structures in PDB]]

PMID:7607225

2007-11-26T17:36:28Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Sprenger, GA, Schörken, U, Sprenger, G and Sahm, H''' (1995) Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains.''Eur. J. Biochem.'' '''230''':525-32

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Transketolase A was purified to apparent homogeneity from recombinant Escherichia coli K12 cells carrying the homologous cloned tktA gene on a pUC19-derived plasmid. These recombinant cells exhibited a transketolase activity in crude extracts of up to 9.7 U/mg compared to < or = 0.1 U/mg in wild-type cells. Transketolase A was purified from crude extracts of a recombinant strain by successive ammonium sulfate precipitations and two anion-exchange chromatography steps (Q-Sepharose FF, Fractogel EMD-DEAE column) and afforded an apparently homogeneous protein band on SDS/PAGE. The enzyme, both in its active and apoform, had a molecular mass of 145,000 Da (+/- 10,000 Da), judged by gel-filtration chromatography. Subunits of 73,000 Da (+/- 2000 Da) were determined on SDS/PAGE, thus, transketolase A most likely forms a homodimer. N-terminal amino acid sequencing of the protein verified the identity with the cloned gene tktA. The specific activity of the purified enzyme, determined at 30 degrees C with the substrates xylulose 5-phosphate (donor of C2 compound) and ribose 5-phosphate (acceptor) at an optimal pH (50 mM glycylglycine, pH 8.5), was 50.4 U/mg. Km values for the substrates xylulose 5-phosphate and ribose 5-phosphate were 160 microM and 1.4 mM, respectively. Km values for the other physiological substrates of transketolase A were 90 microM for erythrose 4-phosphate (best acceptor substrate), 2.1 mM for D,L-glyceraldehyde 3-phosphate, 1.1 mM for fructose 6-phosphate, and 4 mM for sedoheptulose 7-phosphate. Hydroxypyruvate served as alternative donor (Km = 18 mM). Unphosphorylated acceptor compounds were formaldehyde (Km = 31 mM), glycolaldehyde (14 mM), D,L-glyceraldehyde (10 mM) and D-erythrose (150 mM). The enzyme was competitively inhibited by D-arabinose 5-phosphate (K = 6 mM at a concentration of 2.5 mM D-arabinose 5-phosphate) or by the chelating agent EDTA. The inactive apoform of transketolase A was yielded by dialysis against buffer containing 10 mM EDTA, thus removing the cofactors thiamine diphosphate and divalent cations. The reconstitution of the apoenzyme proceded faster in the presence of manganese ions (Kd = 7 microM at 10 microM thiamine diphosphate) than with other divalent cations.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7607225 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221904'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Transketolase
|

|
GO:0004802
|
transketolase activity
|
IDA: Inferred from Direct Assay
|

|
F
|
See Table 2.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.W474b03cec75b1&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:7607225

2007-11-26T17:35:11Z

Michelle: New PMID: Page!

<protect>
{{RightTOC}}

 '''Sprenger, GA, Schörken, U, Sprenger, G and Sahm, H''' (1995) Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains.''Eur. J. Biochem.'' '''230''':525-32

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Transketolase A was purified to apparent homogeneity from recombinant Escherichia coli K12 cells carrying the homologous cloned tktA gene on a pUC19-derived plasmid. These recombinant cells exhibited a transketolase activity in crude extracts of up to 9.7 U/mg compared to < or = 0.1 U/mg in wild-type cells. Transketolase A was purified from crude extracts of a recombinant strain by successive ammonium sulfate precipitations and two anion-exchange chromatography steps (Q-Sepharose FF, Fractogel EMD-DEAE column) and afforded an apparently homogeneous protein band on SDS/PAGE. The enzyme, both in its active and apoform, had a molecular mass of 145,000 Da (+/- 10,000 Da), judged by gel-filtration chromatography. Subunits of 73,000 Da (+/- 2000 Da) were determined on SDS/PAGE, thus, transketolase A most likely forms a homodimer. N-terminal amino acid sequencing of the protein verified the identity with the cloned gene tktA. The specific activity of the purified enzyme, determined at 30 degrees C with the substrates xylulose 5-phosphate (donor of C2 compound) and ribose 5-phosphate (acceptor) at an optimal pH (50 mM glycylglycine, pH 8.5), was 50.4 U/mg. Km values for the substrates xylulose 5-phosphate and ribose 5-phosphate were 160 microM and 1.4 mM, respectively. Km values for the other physiological substrates of transketolase A were 90 microM for erythrose 4-phosphate (best acceptor substrate), 2.1 mM for D,L-glyceraldehyde 3-phosphate, 1.1 mM for fructose 6-phosphate, and 4 mM for sedoheptulose 7-phosphate. Hydroxypyruvate served as alternative donor (Km = 18 mM). Unphosphorylated acceptor compounds were formaldehyde (Km = 31 mM), glycolaldehyde (14 mM), D,L-glyceraldehyde (10 mM) and D-erythrose (150 mM). The enzyme was competitively inhibited by D-arabinose 5-phosphate (K = 6 mM at a concentration of 2.5 mM D-arabinose 5-phosphate) or by the chelating agent EDTA. The inactive apoform of transketolase A was yielded by dialysis against buffer containing 10 mM EDTA, thus removing the cofactors thiamine diphosphate and divalent cations. The reconstitution of the apoenzyme proceded faster in the presence of manganese ions (Kd = 7 microM at 10 microM thiamine diphosphate) than with other divalent cations.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7607225 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221904'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.W474b03cec75b1&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

tktA:Gene Product(s)

2007-11-26T17:34:32Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|tktA}}{{Tab|Gene|tktA}}{{Tab On|Gene Product(s)|tktA}}{{Tab|Expression|tktA}}{{Tab|Evolution|tktA}}{{Tab|On One Page|tktA}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
TktA product
|-
!{{table heading style}} |Synonyms
|
transketolase 1, thiamin-binding product<ref name='LIB:Riley_2006'/>, B2935 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Tkt product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, TktA product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
TktA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:transketolase I|transketolase I]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=2.2.1.1 2.2.1.1]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.D46aac7d5f3f9c&page=26249&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='172963'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0016052
|
carbohydrate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009052
|
pentose-phosphate shunt, non-oxidative branch
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0015949
|
nucleobase, nucleoside and nucleotide interconversion
|

|

|

|
P
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0004802
|
transketolase activity
|
[[PMID:8396116]]<ref name=PMID:8396116/>
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
complete
|-
|

|
GO:0004802
|
transketolase activity
|
[[PMID:7607225]]<ref name=PMID:7607225/>
|
IDA: Inferred from Direct Assay
|

|
F
|

|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.M46aac7d76ff97&page=26249&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='172964'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:transketolase I|transketolase I]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.F46aac7efe5974&page=26249&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='117213'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.G46a85d4df3fc9&page=26249&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=TRANSKETOI-MONOMER at EcoCyc]
<pre>MSSRKELANA IRALSMDAVQ KAKSGHPGAP MGMADIAEVL WRDFLKHNPQ NPSWADRDRF
VLSNGHGSML IYSLLHLTGY DLPMEELKNF RQLHSKTPGH PEVGYTAGVE TTTGPLGQGI
ANAVGMAIAE KTLAAQFNRP GHDIVDHYTY AFMGDGCMME GISHEVCSLA GTLKLGKLIA
FYDDNGISID GHVEGWFTDD TAMRFEAYGW HVIRDIDGHD AASIKRAVEE ARAVTDKPSL
LMCKTIIGFG SPNKAGTHDS HGAPLGDAEI ALTREQLGWK YAPFEIPSEI YAQWDAKEAG
QAKESAWNEK FAAYAKAYPQ EAAEFTRRMK GEMPSDFDAK AKEFIAKLQA NPAKIASRKA
SQNAIEAFGP LLPEFLGGSA DLAPSNLTLW SGSKAINEDA AGNYIHYGVR EFGMTAIANG
ISLHGGFLPY TSTFLMFVEY ARNAVRMAAL MKQRQVMVYT HDSIGLGEDG PTHQPVEQVA
SLRVTPNMST WRPCDQVESA VAWKYGVERQ DGPTALILSR QNLAQQERTE EQLANIARGG
YVLKDCAGQP ELIFIATGSE VELAVAAYEK LTAEGVKARV VSMPSTDAFD KQDAAYRESV
LPKAVTARVA VEAGIADYWY KYVGLNGAIV GMTTFGESAP AELLFEEFGF TVDNVVAKAK ELL</pre>
|-
!{{table heading style}} |Mol. Wt
|
72.21 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
94770 - 95395 (calc based on 23 Y, 11 W, and 5 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.O46aac7f24d8c7&page=26249&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='172966'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.P46aac7f2bdd47&page=26249&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='172967'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1QGD 1QGD] TRANSKETOLASE FROM ESCHERICHIA COLI
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.D46aac7f328998&page=26249&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='172968'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.L46aac7f41204b&page=26249&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='172969'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=TRANSKETOI-MONOMER EcoCyc:TRANSKETOI-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P27302 UniProt:P27302]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00456 PFAM:PF00456]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=YP_026188 RefSeq:YP_026188]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P27302 ModBase:P27302]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1QGD PDB:1QGD]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.O46aac7f471ace&page=26249&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='117214'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.Y46a85d543f2d0&page=26249&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0016052_!_carbohydrate catabolic process]][[Category:GO:0009052_!_pentose-phosphate shunt, non-oxidative branch]][[Category:GO:0015949_!_nucleobase, nucleoside and nucleotide interconversion]][[Category:GO:0004802_!_transketolase activity]][[Category:Complex:transketolase I]][[Category:Products with structures in PDB]]

tktA:Gene Product(s)

2007-11-26T17:33:28Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|tktA}}{{Tab|Gene|tktA}}{{Tab On|Gene Product(s)|tktA}}{{Tab|Expression|tktA}}{{Tab|Evolution|tktA}}{{Tab|On One Page|tktA}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
TktA product
|-
!{{table heading style}} |Synonyms
|
transketolase 1, thiamin-binding product<ref name='LIB:Riley_2006'/>, B2935 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Tkt product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, TktA product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
TktA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:transketolase I|transketolase I]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=2.2.1.1 2.2.1.1]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.D46aac7d5f3f9c&page=26249&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='172963'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0016052
|
carbohydrate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009052
|
pentose-phosphate shunt, non-oxidative branch
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0015949
|
nucleobase, nucleoside and nucleotide interconversion
|

|

|

|
P
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0004802
|
transketolase activity
|
[[PMID:8396116]]<ref name=PMID:8396116/>
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.M46aac7d76ff97&page=26249&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='172964'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:transketolase I|transketolase I]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.F46aac7efe5974&page=26249&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='117213'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.G46a85d4df3fc9&page=26249&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=TRANSKETOI-MONOMER at EcoCyc]
<pre>MSSRKELANA IRALSMDAVQ KAKSGHPGAP MGMADIAEVL WRDFLKHNPQ NPSWADRDRF
VLSNGHGSML IYSLLHLTGY DLPMEELKNF RQLHSKTPGH PEVGYTAGVE TTTGPLGQGI
ANAVGMAIAE KTLAAQFNRP GHDIVDHYTY AFMGDGCMME GISHEVCSLA GTLKLGKLIA
FYDDNGISID GHVEGWFTDD TAMRFEAYGW HVIRDIDGHD AASIKRAVEE ARAVTDKPSL
LMCKTIIGFG SPNKAGTHDS HGAPLGDAEI ALTREQLGWK YAPFEIPSEI YAQWDAKEAG
QAKESAWNEK FAAYAKAYPQ EAAEFTRRMK GEMPSDFDAK AKEFIAKLQA NPAKIASRKA
SQNAIEAFGP LLPEFLGGSA DLAPSNLTLW SGSKAINEDA AGNYIHYGVR EFGMTAIANG
ISLHGGFLPY TSTFLMFVEY ARNAVRMAAL MKQRQVMVYT HDSIGLGEDG PTHQPVEQVA
SLRVTPNMST WRPCDQVESA VAWKYGVERQ DGPTALILSR QNLAQQERTE EQLANIARGG
YVLKDCAGQP ELIFIATGSE VELAVAAYEK LTAEGVKARV VSMPSTDAFD KQDAAYRESV
LPKAVTARVA VEAGIADYWY KYVGLNGAIV GMTTFGESAP AELLFEEFGF TVDNVVAKAK ELL</pre>
|-
!{{table heading style}} |Mol. Wt
|
72.21 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
94770 - 95395 (calc based on 23 Y, 11 W, and 5 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.O46aac7f24d8c7&page=26249&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='172966'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.P46aac7f2bdd47&page=26249&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='172967'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1QGD 1QGD] TRANSKETOLASE FROM ESCHERICHIA COLI
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.D46aac7f328998&page=26249&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='172968'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.L46aac7f41204b&page=26249&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='172969'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=TRANSKETOI-MONOMER EcoCyc:TRANSKETOI-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P27302 UniProt:P27302]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00456 PFAM:PF00456]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=YP_026188 RefSeq:YP_026188]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P27302 ModBase:P27302]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1QGD PDB:1QGD]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.O46aac7f471ace&page=26249&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='117214'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26249.Y46a85d543f2d0&page=26249&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0016052_!_carbohydrate catabolic process]][[Category:GO:0009052_!_pentose-phosphate shunt, non-oxidative branch]][[Category:GO:0015949_!_nucleobase, nucleoside and nucleotide interconversion]][[Category:GO:0004802_!_transketolase activity]][[Category:Complex:transketolase I]][[Category:Products with structures in PDB]]

PMID:8396116

2007-11-26T17:32:41Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Iida, A, Teshiba, S and Mizobuchi, K''' (1993) Identification and characterization of the tktB gene encoding a second transketolase in Escherichia coli K-12.''J. Bacteriol.'' '''175''':5375-83

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || We isolated a transposon Tn10 insertion mutant of Escherichia coli K-12 which could not grow on MacConkey plates containing D-ribose. Characterization of the mutant revealed that the level of the transketolase activity was reduced to one-third of that of the wild type. The mutation was mapped at 63.5 min on the E. coli genetic map, in which the transketolase gene (tkt) had been mapped. A multicopy suppressor gene which complemented the tkt mutation was cloned on a 7.8-kb PstI fragment. The cloned gene was located at 53 min on the chromosome. Subcloning and sequencing of a 2.7-kb fragment containing the suppressor gene identified an open reading frame encoding a polypeptide of 667 amino acids with a calculated molecular weight of 72,973. Overexpression of the protein and determination of its N-terminal amino acid sequence defined unambiguously the translational start site of the gene. The deduced amino acid sequence showed similarity to sequences of transketolases from Saccharomyces cerevisiae and Rhodobacter sphaeroides. In addition, the level of the transketolase activity increased in strains carrying the gene in multicopy. Therefore, the gene encoding this transketolase was designated tktB and the gene formerly called tkt was renamed tktA. Analysis of the phenotypes of the strains containing tktA, tktB, or tktA tktB mutations indicated that tktA and tktB were responsible for major and minor activities, respectively, of transketolase in E. coli.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8396116 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221903'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Transketolase
|

|
GO:0004802
|
transketolase activity
|
IDA: Inferred from Direct Assay
|

|
F
|
See Table 2.
|
complete
|-
|
Transketolase
|

|
GO:0004802
|
transketolase activity
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
See Figure 6 and "Phenotypes of the tktA and tktB mutations" paragraph.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.G474b023add4d4&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:8396116

2007-11-26T17:28:27Z

Michelle: New PMID: Page!

<protect>
{{RightTOC}}

 '''Iida, A, Teshiba, S and Mizobuchi, K''' (1993) Identification and characterization of the tktB gene encoding a second transketolase in Escherichia coli K-12.''J. Bacteriol.'' '''175''':5375-83

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || We isolated a transposon Tn10 insertion mutant of Escherichia coli K-12 which could not grow on MacConkey plates containing D-ribose. Characterization of the mutant revealed that the level of the transketolase activity was reduced to one-third of that of the wild type. The mutation was mapped at 63.5 min on the E. coli genetic map, in which the transketolase gene (tkt) had been mapped. A multicopy suppressor gene which complemented the tkt mutation was cloned on a 7.8-kb PstI fragment. The cloned gene was located at 53 min on the chromosome. Subcloning and sequencing of a 2.7-kb fragment containing the suppressor gene identified an open reading frame encoding a polypeptide of 667 amino acids with a calculated molecular weight of 72,973. Overexpression of the protein and determination of its N-terminal amino acid sequence defined unambiguously the translational start site of the gene. The deduced amino acid sequence showed similarity to sequences of transketolases from Saccharomyces cerevisiae and Rhodobacter sphaeroides. In addition, the level of the transketolase activity increased in strains carrying the gene in multicopy. Therefore, the gene encoding this transketolase was designated tktB and the gene formerly called tkt was renamed tktA. Analysis of the phenotypes of the strains containing tktA, tktB, or tktA tktB mutations indicated that tktA and tktB were responsible for major and minor activities, respectively, of transketolase in E. coli.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8396116 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221903'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.G474b023add4d4&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

tktB:Gene Product(s)

2007-11-26T17:28:16Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|tktB}}{{Tab|Gene|tktB}}{{Tab On|Gene Product(s)|tktB}}{{Tab|Expression|tktB}}{{Tab|Evolution|tktB}}{{Tab|On One Page|tktB}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
TktB product
|-
!{{table heading style}} |Synonyms
|
transketolase 2, thiamin-binding product<ref name='LIB:Riley_2006'/>, B2465 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, TktB product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
TRANSKETOII-MONOMER<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:transketolase II|transketolase II]]<ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=2.2.1.1 2.2.1.1]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25171.Z46aaa918f1be1&page=25171&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='169564'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0016052
|
carbohydrate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009052
|
pentose-phosphate shunt, non-oxidative branch
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0015949
|
nucleobase, nucleoside and nucleotide interconversion
|

|

|

|
P
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0004802
|
transketolase activity
|
[[PMID:8396116]]<ref name=PMID:8396116/>
|
IDA: Inferred from Direct Assay
|

|
F
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
complete
|-
|

|
GO:0004802
|
transketolase activity
|
[[PMID:8396116]]<ref name=PMID:8396116/>
|
IMP: Inferred from Mutant Phenotype
|

|
F
|

|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25171.L46aaa91a67d5c&page=25171&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='169565'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:transketolase II|transketolase II]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25171.O46aaa932a45c5&page=25171&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='114976'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25171.X46a841abac7a6&page=25171&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=TRANSKETOII-MONOMER at EcoCyc]
<pre>MSRKDLANAI RALSMDAVQK ANSGHPGAPM GMADIAEVLW NDFLKHNPTD PTWYDRDRFI
LSNGHASMLL YSLLHLTGYD LPLEELKNFR QLHSKTPGHP EIGYTPGVET TTGPLGQGLA
NAVGLAIAER TLAAQFNQPD HEIVDHFTYV FMGDGCLMEG ISHEVCSLAG TLGLGKLIGF
YDHNGISIDG ETEGWFTDDT AKRFEAYHWH VIHEIDGHDP QAVKEAILEA QSVKDKPSLI
ICRTVIGFGS PNKAGKEEAH GAPLGEEEVA LARQKLGWHH PPFEIPKEIY HAWDAREKGE
KAQQSWNEKF AAYKKAHPQL AEEFTRRMSG GLPKDWEKTT QKYINELQAN PAKIATRKAS
QNTLNAYGPM LPELLGGSAD LAPSNLTIWK GSVSLKEDPA GNYIHYGVRE FGMTAIANGI
AHHGGFVPYT ATFLMFVEYA RNAARMAALM KARQIMVYTH DSIGLGEDGP THQAVEQLAS
LRLTPNFSTW RPCDQVEAAV GWKLAVERHN GPTALILSRQ NLAQVERTPD QVKEIARGGY
VLKDSGGKPD IILIATGSEM EITLQAAEKL AGEGRNVRVV SLPSTDIFDA QDEEYRESVL
PSNVAARVAV EAGIADYWYK YVGLKGAIVG MTGYGESAPA DKLFPFFGFT AENIVAKAHK
VLGVKGA</pre>
|-
!{{table heading style}} |Mol. Wt
|
73.04 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
98780 - 99280 (calc based on 22 Y, 12 W, and 4 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25171.E46aaa935078e3&page=25171&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='169567'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25171.I46aaa93576b5f&page=25171&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='114977'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25171.D46a841ad797d4&page=25171&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='169568'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25171.B46aaa9363efaa&page=25171&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='169569'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=TRANSKETOII-MONOMER EcoCyc:TRANSKETOII-MONOMER]
|

|-
|
[http://swissmodel.expasy.org/repository/ SwissModel] ([[SwissModel|EcoliWiki Page]])
|
[http://swissmodel.expasy.org/repository/smr.php?job=2&sptr_ac=P33570 SwissModel:P33570]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P33570 UniProt:P33570]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00456 PFAM:PF00456]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_416960 RefSeq:NP_416960]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P33570 ModBase:P33570]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25171.D46aaa9369ca3c&page=25171&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='114978'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.25171.Y46a841b219f4b&page=25171&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0016052_!_carbohydrate catabolic process]][[Category:GO:0009052_!_pentose-phosphate shunt, non-oxidative branch]][[Category:GO:0015949_!_nucleobase, nucleoside and nucleotide interconversion]][[Category:GO:0004802_!_transketolase activity]][[Category:Complex:transketolase II]]

PMID:4869212

2007-11-26T17:14:54Z

Michelle: edited by Michelle via TableEdit

<protect>
{{RightTOC}}

 '''Fraenkel, DG''' (1968) Selection of Escherichia coli mutants lacking glucose-6-phosphate dehydrogenase or gluconate-6-phosphate dehydrogenase.''J. Bacteriol.'' '''95''':1267-71

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Glucose is metabolized in Escherichia coli chiefly via the phosphoglucose isomerase reaction; mutants lacking that enzyme grow slowly on glucose by using the hexose monophosphate shunt. When such a strain is further mutated so as to yield strains unable to grow at all on glucose or on glucose-6-phosphate, the secondary strains are found to lack also activity of glucose-6-phosphate dehydrogenase. The double mutants can be transduced back to glucose positivity; one class of transductants has normal phosphoglucose isomerase activity but no glucose-6-phosphate dehydrogenase. An analogous scheme has been used to select mutants lacking gluconate-6-phosphate dehydrogenase. Here the primary mutant lacks gluconate-6-phosphate dehydrase (an enzyme of the Enter-Doudoroff pathway) and grows slowly on gluconate; gluconate-negative mutants are selected from it. These mutants, lacking the nicotinamide dinucleotide phosphate-linked glucose-6-phosphate dehydrogenase or gluconate-6-phosphate dehydrogenase, grow on glucose at rates similar to the wild type. Thus, these enzymes are not essential for glucose metabolism in E. coli.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4869212 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221902'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Glucose-6-Phosphate Dehydrogenase
|

|
GO:0004345
|
glucose-6-phosphate dehydrogenase activity
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
See Table 1.
|
complete
|-
|
Gluconate-6-Phosphate Dehydrogenase
|

|
GO:0004616
|
phosphogluconate dehydrogenase (decarboxylating) activity
|
IMP: Inferred from Mutant Phenotype
|

|
F
|
See Table 2.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.V474afd9594894&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

gnd:Gene Product(s)

2007-11-26T17:13:43Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|gnd}}{{Tab|Gene|gnd}}{{Tab On|Gene Product(s)|gnd}}{{Tab|Expression|gnd}}{{Tab|Evolution|gnd}}{{Tab|On One Page|gnd}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
Gnd product
|-
!{{table heading style}} |Synonyms
|
gluconate-6-phosphate dehydrogenase, decarboxylating product<ref name='LIB:Riley_2006'/>, B2029 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Gnd product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
Gnd<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:6-phosphogluconate dehydrogenase (decarboxylating)|6-phosphogluconate dehydrogenase (decarboxylating)]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=1.1.1.44 1.1.1.44]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24191.N46aa8d4d31ec5&page=24191&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='166386'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0016052
|
carbohydrate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009051
|
pentose-phosphate shunt, oxidative branch
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009052
|
pentose-phosphate shunt, non-oxidative branch
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0004616
|
phosphogluconate dehydrogenase (decarboxylating) activity
|
[[PMID:4869212]]<ref name=PMID:4869212/>
|
IMP: Inferred from Mutant Phenotype
|

|
F
|

|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24191.Q46aa8d4e98df8&page=24191&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='166387'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:6-phosphogluconate dehydrogenase (decarboxylating)|6-phosphogluconate dehydrogenase (decarboxylating)]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24191.F46aa8d655b272&page=24191&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='112746'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24191.R46a820b641ebf&page=24191&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=6PGLUCONDEHYDROG-MONOMER at EcoCyc]
<pre>MSKQQIGVVG MAVMGRNLAL NIESRGYTVS IFNRSREKTE EVIAENPGKK LVPYYTVKEF
VESLETPRRI LLMVKAGAGT DAAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF
NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILTKIA AVAEDGEPCV TYIGADGAGH
YVKMVHNGIE YGDMQLIAEA YSLLKGGLNL TNEELAQTFT EWNNGELSSY LIDITKDIFT
KKDEDGNYLV DVILDEAANK GTGKWTSQSA LDLGEPLSLI TESVFARYIS SLKDQRVAAS
KVLSGPQAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASEEYNWD LNYGEIAKIF
RAGCIIRAQF LQKITDAYAE NPQIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIPVPT
FSAAVAYYDS YRAAVLPANL IQAQRDYFGA HTYKRIDKEG VFHTEWLD</pre>
|-
!{{table heading style}} |Mol. Wt
|
51.48 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|
5.3<ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |Extinction coefficient
|
59250 - 59500 (calc based on 25 Y, 4 W, and 2 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24191.D46aa8d67ac6ab&page=24191&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='166389'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24191.E46aa8d6824c7a&page=24191&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='112748'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24191.G46a820b81a567&page=24191&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='166390'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24191.Y46aa8d68ddcb7&page=24191&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='166391'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=6PGLUCONDEHYDROG-MONOMER EcoCyc:6PGLUCONDEHYDROG-MONOMER]
|

|-
|
[http://swissmodel.expasy.org/repository/ SwissModel] ([[SwissModel|EcoliWiki Page]])
|
[http://swissmodel.expasy.org/repository/smr.php?job=2&sptr_ac=P00350 SwissModel:P00350]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P00350 UniProt:P00350]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF03446 PFAM:PF03446]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_416533 RefSeq:NP_416533]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P00350 ModBase:P00350]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24191.C46aa8d6945eaa&page=24191&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='112751'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24191.Z46a820bc955b3&page=24191&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0016052_!_carbohydrate catabolic process]][[Category:GO:0009051_!_pentose-phosphate shunt, oxidative branch]][[Category:GO:0009052_!_pentose-phosphate shunt, non-oxidative branch]][[Category:Complex:6-phosphogluconate dehydrogenase (decarboxylating)]]

PMID:4869212

2007-11-26T17:08:38Z

Michelle: New PMID: Page!

<protect>
{{RightTOC}}

 '''Fraenkel, DG''' (1968) Selection of Escherichia coli mutants lacking glucose-6-phosphate dehydrogenase or gluconate-6-phosphate dehydrogenase.''J. Bacteriol.'' '''95''':1267-71

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || Glucose is metabolized in Escherichia coli chiefly via the phosphoglucose isomerase reaction; mutants lacking that enzyme grow slowly on glucose by using the hexose monophosphate shunt. When such a strain is further mutated so as to yield strains unable to grow at all on glucose or on glucose-6-phosphate, the secondary strains are found to lack also activity of glucose-6-phosphate dehydrogenase. The double mutants can be transduced back to glucose positivity; one class of transductants has normal phosphoglucose isomerase activity but no glucose-6-phosphate dehydrogenase. An analogous scheme has been used to select mutants lacking gluconate-6-phosphate dehydrogenase. Here the primary mutant lacks gluconate-6-phosphate dehydrase (an enzyme of the Enter-Doudoroff pathway) and grows slowly on gluconate; gluconate-negative mutants are selected from it. These mutants, lacking the nicotinamide dinucleotide phosphate-linked glucose-6-phosphate dehydrogenase or gluconate-6-phosphate dehydrogenase, grow on glucose at rates similar to the wild type. Thus, these enzymes are not essential for glucose metabolism in E. coli.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4869212 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221902'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.V474afd9594894&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

zwf:Gene Product(s)

2007-11-26T17:07:42Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|zwf}}{{Tab|Gene|zwf}}{{Tab On|Gene Product(s)|zwf}}{{Tab|Expression|zwf}}{{Tab|Evolution|zwf}}{{Tab|On One Page|zwf}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
Zwf product
|-
!{{table heading style}} |Synonyms
|
glucose-6-phosphate dehydrogenase product<ref name='LIB:Riley_2006'/>, B1852 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Zwf product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, G6PDH product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
GLU6PDEHYDROG-MONOMER<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23807.J46aa81bc1d426&page=23807&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='165134'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0016052
|
carbohydrate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009051
|
pentose-phosphate shunt, oxidative branch
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0004345
|
glucose-6-phosphate dehydrogenase activity
|
[[PMID:4869212]]<ref name=PMID:4869212/>
|
IMP: Inferred from Mutant Phenotype
|

|
F
|

|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23807.L46aa81bd28f48&page=23807&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='165135'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23807.L46aa81d0139b5&page=23807&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='111675'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23807.L46a81291ecf32&page=23807&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=GLU6PDEHYDROG-MONOMER at EcoCyc]
<pre>MAVTQTAQAC DLVIFGAKGD LARRKLLPSL YQLEKAGQLN PDTRIIGVGR ADWDKAAYTK
VVREALETFM KETIDEGLWD TLSARLDFCN LDVNDTAAFS RLGAMLDQKN RITINYFAMP
PSTFGAICKG LGEAKLNAKP ARVVMEKPLG TSLATSQEIN DQVGEYFEEC QVYRIDHYLG
KETVLNLLAL RFANSLFVNN WDNRTIDHVE ITVAEEVGIE GRWGYFDKAG QMRDMIQNHL
LQILCMIAMS PPSDLSADSI RDEKVKVLKS LRRIDRSNVR EKTVRGQYTA GFAQGKKVPG
YLEEEGANKS SNTETFVAIR VDIDNWRWAG VPFYLRTGKR LPTKCSEVVV YFKTPELNLF
KESWQDLPQN KLTIRLQPDE GVDIQVLNKV PGLDHKHNLQ ITKLDLSYSE TFNQTHLADA
YERLLLETMR GIQALFVRRD EVEEAWKWVD SITEAWAMDN DAPKPYQAGT WGPVASVAMI
TRDGRSWNEF E</pre>
|-
!{{table heading style}} |Mol. Wt
|
55.7 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|
5.89<ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |Extinction coefficient
|
86860 - 87610 (calc based on 14 Y, 12 W, and 6 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23807.H46aa81d1e9e97&page=23807&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='165137'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23807.E46aa81d261ab5&page=23807&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='111677'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23807.E46a81293e49c6&page=23807&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='165138'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23807.D46aa81d3258ba&page=23807&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='165139'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=GLU6PDEHYDROG-MONOMER EcoCyc:GLU6PDEHYDROG-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0AC53 UniProt:P0AC53]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00479 PFAM:PF00479]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_416366 RefSeq:NP_416366]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P0AC53 ModBase:P0AC53]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23807.K46aa81d3810e0&page=23807&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='111682'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23807.B46a812978c9f7&page=23807&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0016052_!_carbohydrate catabolic process]][[Category:GO:0009051_!_pentose-phosphate shunt, oxidative branch]]

talB:Gene Product(s)

2007-11-07T22:00:10Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|talB}}{{Tab|Gene|talB}}{{Tab On|Gene Product(s)|talB}}{{Tab|Expression|talB}}{{Tab|Evolution|talB}}{{Tab|On One Page|talB}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
TalB product
|-
!{{table heading style}} |Synonyms
|
transaldolase B product<ref name='LIB:Riley_2006'/>, B0008 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, YaaK product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, TalB product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
transaldolase B<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:transaldolase B|transaldolase B]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19407.D46aa14e206d54&page=19407&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='151442'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009052
|
pentose-phosphate shunt, non-oxidative branch
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0004801
|
transaldolase activity
|
[[PMID:7592346]]<ref name=PMID:7592346/>
|
IDA: Inferred from Direct Assay
|

|
F
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19407.A46aa14e35aa5c&page=19407&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='151443'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:transaldolase B|transaldolase B]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19407.Z46aa14f220f68&page=19407&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='100599'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19407.T46a72adfda1c5&page=19407&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=TRANSALDOLB-MONOMER at EcoCyc]
<pre>MTDKLTSLRQ YTTVVADTGD IAAMKLYQPQ DATTNPSLIL NAAQIPEYRK LIDDAVAWAK
QQSNDRAQQI VDATDKLAVN IGLEILKLVP GRISTEVDAR LSYDTEASIA KAKRLIKLYN
DAGISNDRIL IKLASTWQGI RAAEQLEKEG INCNLTLLFS FAQARACAEA GVFLISPFVG
RILDWYKANT DKKEYAPAED PGVVSVSEIY QYYKEHGYET VVMGASFRNI GEILELAGCD
RLTIAPALLK ELAESEGAIE RKLSYTGEVK ARPARITESE FLWQHNQDPM AVDKLAEGIR
KFAIDQEKLE KMIGDLL</pre>
|-
!{{table heading style}} |Mol. Wt
|
35.22 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|
5.31<ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |Extinction coefficient
|
39880 - 40255 (calc based on 12 Y, 4 W, and 3 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19407.C46aa14f432a17&page=19407&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='151445'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19407.L46aa14f48a2fc&page=19407&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='151446'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1UCW 1UCW] COMPLEX OF TRANSALDOLASE WITH THE REDUCED SCHIFF-BASE INTERMEDIATE
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1I2N 1I2N] CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT N35A
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1I2O 1I2O] CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT E96A
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1I2P 1I2P] CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT D17A
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1I2Q 1I2Q] CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT T156A
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1I2R 1I2R] CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT S176A
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1ONR 1ONR] STRUCTURE OF TRANSALDOLASE B
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19407.Z46aa14f4d236c&page=19407&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='151447'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19407.I46aa14f9855a0&page=19407&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='151448'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=TRANSALDOLB-MONOMER EcoCyc:TRANSALDOLB-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0A870 UniProt:P0A870]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00923 PFAM:PF00923]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_414549 RefSeq:NP_414549]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P0A870 ModBase:P0A870]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1ONR PDB:1ONR]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19407.U46aa14f9cdfa9&page=19407&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='100600'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19407.L46a72ae958b2a&page=19407&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0009052_!_pentose-phosphate shunt, non-oxidative branch]][[Category:GO:0004801_!_transaldolase activity]][[Category:Complex:transaldolase B]][[Category:Products with structures in PDB]]

rpiA:Gene Product(s)

2007-11-07T21:59:10Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|rpiA}}{{Tab|Gene|rpiA}}{{Tab On|Gene Product(s)|rpiA}}{{Tab|Expression|rpiA}}{{Tab|Evolution|rpiA}}{{Tab|On One Page|rpiA}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
RpiA product
|-
!{{table heading style}} |Synonyms
|
ribose 5-phosphate isomerase, constitutive product<ref name='LIB:Riley_2006'/>, B2914 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, YgfC product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, RpiA product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
ribose-5-phosphate isomerase A<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:ribose-5-phosphate isomerase A|ribose-5-phosphate isomerase A]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26204.V46aac68f091f3&page=26204&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='172814'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0016052
|
carbohydrate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009052
|
pentose-phosphate shunt, non-oxidative branch
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0004751
|
ribose-5-phosphate isomerase activity
|
[[PMID:8366047]]<ref name=PMID:8366047/>
|
IMP: Inferred from Mutant Phenotype
|

|
F
|

|
complete
|-
|

|
GO:0004751
|
ribose-5-phosphate isomerase activity
|
[[PMID:8366047]]<ref name=PMID:8366047/>
|
IDA: Inferred from Direct Assay
|

|
F
|

|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26204.X46aac6907842a&page=26204&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='172815'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:ribose-5-phosphate isomerase A|ribose-5-phosphate isomerase A]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26204.B46aac69f6d5b2&page=26204&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='117162'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26204.Q46a85c30f2290&page=26204&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=RIB5PISOMA-MONOMER at EcoCyc]
<pre>MTQDELKKAV GWAALQYVQP GTIVGVGTGS TAAHFIDALG TMKGQIEGAV SSSDASTEKL
KSLGIHVFDL NEVDSLGIYV DGADEINGHM QMIKGGGAAL TREKIIASVA EKFICIADAS
KQVDILGKFP LPVEVIPMAR SAVARQLVKL GGRPEYRQGV VTDNGNVILD VHGMEILDPI
AMENAINAIP GVVTVGLFAN RGADVALIGT PDGVKTIVK</pre>
|-
!{{table heading style}} |Mol. Wt
|
22.86 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
9970 - 10095 (calc based on 3 Y, 1 W, and 1 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26204.K46aac6a1c85e4&page=26204&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='172817'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26204.W46aac6a2448b3&page=26204&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='172818'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1LKZ 1LKZ] Crystal structure of D-ribose-5-phosphate isomerase (RpiA) from Escherichia coli.
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KS2 1KS2] Crystal Structure Analysis of the rpiA, Structural Genomics, protein EC1268.
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26204.H46aac6a2a343e&page=26204&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='172819'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26204.G46aac6a4265fa&page=26204&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='172820'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=RIB5PISOMA-MONOMER EcoCyc:RIB5PISOMA-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0A7Z0 UniProt:P0A7Z0]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF06026 PFAM:PF06026]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_417389 RefSeq:NP_417389]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P0A7Z0 ModBase:P0A7Z0]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KS2 PDB:1KS2]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26204.E46aac6a485d44&page=26204&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='117163'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26204.K46a85c37cee2a&page=26204&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0016052_!_carbohydrate catabolic process]][[Category:GO:0009052_!_pentose-phosphate shunt, non-oxidative branch]][[Category:Complex:ribose-5-phosphate isomerase A]][[Category:Products with structures in PDB]]

PMID:4945194

2007-10-31T21:02:07Z

Michelle: New PMID: Page!

<protect>
{{RightTOC}}

 '''Fradkin, JE and Fraenkel, DG''' (1971) 2-keto-3-deoxygluconate 6-phosphate aldolase mutants of Escherichia coli.''J. Bacteriol.'' '''108''':1277-83

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || A new mutation in Escherichia coli, giving inability to grow on gluconic, glucuronic, or galacturonic acids, has been identified as complete deficiency of 2-keto-3-deoxygluconate 6-phosphate (KDGP) aldolase activity. The genetic map position of the locus, eda, is about 35 min. The inability to grow on the uronic acids was expected, because the aldolase is on the sole known pathway of their metabolism. However, inability to grow on gluconate was less expected, because the hexose monophosphate shunt might be used, as happens in mutants blocked in the previous step, edd, of the Entner-Doudoroff pathway. The likely explanation of gluconate negativity is inhibition by accumulated KDGP, because gluconate is inhibitory to growth on other substances, and one type of gluconate revertant is eda(-), edd(-). KDGP is probably the inducer of KDGP aldolase.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4945194 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221646'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.P4728ed4f78545&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

PMID:5337844

2007-10-31T21:01:50Z

Michelle: New PMID: Page!

<protect>
{{RightTOC}}

 '''Zablotny, R and Fraenkel, DG''' (1967) Glucose and gluconate metabolism in a mutant of Escherichia coli lacking gluconate-6-phosphate dehydrase.''J. Bacteriol.'' '''93''':1579-81

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || A mutant lacking gluconate-6-phosphate dehydrase (the first enzyme of the Entner-Doudoroff pathway) was isolated after ethyl methane sulfonate mutagenesis of Escherichia coli. Other enzymes of gluconate metabolism (gluconokinase, gluconate-6-phosphate dehydrogenase, and 2-keto-3-deoxygluconate-6-phosphate aldolase) were present in the mutant. When the mutant was grown on gluconate-1-(14)C, alanine isolated from protein was unlabeled, showing that the dehydrase was absent in vivo and that the sole pathway of gluconate metabolism in the mutant was the hexose monophosphate shunt. The mutant grew on gluconate with a doubling time of 155 min, compared with the parent strain's 56 min. On glucose and fructose it grew with normal doubling times. Thus, in E. coli, the Entner-Doudoroff pathway is used for gluconate metabolism but not for glucose metabolism.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=5337844 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>

{|class = 'sortable' {{Prettytable}} id='221645'
|- {{table heading style}}
!Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.B4728ed3dc73be&page=0&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>

edd:Gene Product(s)

2007-10-31T21:01:38Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|edd}}{{Tab|Gene|edd}}{{Tab On|Gene Product(s)|edd}}{{Tab|Expression|edd}}{{Tab|Evolution|edd}}{{Tab|On One Page|edd}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
Edd product
|-
!{{table heading style}} |Synonyms
|
6-phosphogluconate dehydratase product<ref name='LIB:Riley_2006'/>, B1851 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Edd product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
PGLUCONDEHYDRAT-MONOMER<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=4.2.1.12 4.2.1.12]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23805.N46aa81ac40301&page=23805&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='165127'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0009255
|
Entner-Doudoroff pathway
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0004456
|
phosphogluconate dehydratase activity
|
[[PMID:5337844]]<ref name=PMID:5337844/>
|
IMP: Inferred from Mutant Phenotype
|

|
F
|

|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23805.T46aa81ad4844f&page=23805&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='165128'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23805.R46aa81b4d493e&page=23805&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='111657'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23805.Q46a8127460779&page=23805&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=PGLUCONDEHYDRAT-MONOMER at EcoCyc]
<pre>MNPQLLRVTN RIIERSRETR SAYLARIEQA KTSTVHRSQL ACGNLAHGFA ACQPEDKASL
KSMLRNNIAI ITSYNDMLSA HQPYEHYPEI IRKALHEANA VGQVAGGVPA MCDGVTQGQD
GMELSLLSRE VIAMSAAVGL SHNMFDGALF LGVCDKIVPG LTMAALSFGH LPAVFVPSGP
MASGLPNKEK VRIRQLYAEG KVDRMALLES EAASYHAPGT CTFYGTANTN QMVVEFMGMQ
LPGSSFVHPD SPLRDALTAA AARQVTRMTG NGNEWMPIGK MIDEKVVVNG IVALLATGGS
TNHTMHLVAM ARAAGIQINW DDFSDLSDVV PLMARLYPNG PADINHFQAA GGVPVLVREL
LKAGLLHEDV NTVAGFGLSR YTLEPWLNNG ELDWREGAEK SLDSNVIASF EQPFSHHGGT
KVLSGNLGRA VMKTSAVPVE NQVIEAPAVV FESQHDVMPA FEAGLLDRDC VVVVRHQGPK
ANGMPELHKL MPPLGVLLDR CFKIALVTDG RLSGASGKVP SAIHVTPEAY DGGLLAKVRD
GDIIRVNGQT GELTLLVDEA ELAAREPHIP DLSASRVGTG RELFSALREK LSGAEQGATC ITF</pre>
|-
!{{table heading style}} |Mol. Wt
|
64.64 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
36900 - 37900 (calc based on 10 Y, 4 W, and 8 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23805.H46aa81b6b81b2&page=23805&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='165130'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23805.N46aa81b731f08&page=23805&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='111659'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23805.I46a812763378f&page=23805&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='165131'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23805.U46aa81b7ed8d8&page=23805&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='165132'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=PGLUCONDEHYDRAT-MONOMER EcoCyc:PGLUCONDEHYDRAT-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0ADF6 UniProt:P0ADF6]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00920 PFAM:PF00920]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_416365 RefSeq:NP_416365]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23805.G46aa81b8551a8&page=23805&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='111660'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23805.W46a812792ed2d&page=23805&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0009255_!_Entner-Doudoroff pathway]]

eda:Gene Product(s)

2007-10-31T21:00:38Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|eda}}{{Tab|Gene|eda}}{{Tab On|Gene Product(s)|eda}}{{Tab|Expression|eda}}{{Tab|Evolution|eda}}{{Tab|On One Page|eda}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
Eda product
|-
!{{table heading style}} |Synonyms
|
multifunctional 2-keto-3-deoxygluconate 6-phosphate aldolase and 2-keto-4-hydroxyglutarate aldolase and oxaloacetate decarboxylase product<ref name='LIB:Riley_2006'/>, B1850 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Kga product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Hga product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, KdgA product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Eda product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
Eda<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:KDPGALDOL-4OH2OXOGLUTARALDOL-CPLX|KDPGALDOL-4OH2OXOGLUTARALDOL-CPLX]]<ref name='LIB:EcoCyc10.6'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=4.1.2.16 4.1.2.16]<ref name='LIB:Riley_2006'/>
* [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=4.1.1.3 4.1.1.3]<ref name='LIB:Riley_2006'/>
* [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=4.1.2.14 4.1.2.14]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23802.G46aa8184de2e6&page=23802&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='165119'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0016052
|
carbohydrate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009255
|
Entner-Doudoroff pathway
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009436
|
glyoxylate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0008675
|
2-dehydro-3-deoxy-phosphogluconate aldolase activity
|
[[PMID:4945194]]<ref name=PMID:4945194/>
|
IMP: Inferred from Mutant Phenotype
|

|
F
|

|
complete
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23802.S46aa81865c815&page=23802&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='165120'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:KDPGALDOL-4OH2OXOGLUTARALDOL-CPLX|KDPGALDOL-4OH2OXOGLUTARALDOL-CPLX]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23802.J46aa81a149dfa&page=23802&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='111655'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23802.Z46a81261a95eb&page=23802&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER at EcoCyc]
<pre>MKNWKTSAES ILTTGPVVPV IVVKKLEHAV PMAKALVAGG VRVLEVTLRT ECAVDAIRAI
AKEVPEAIVG AGTVLNPQQL AEVTEAGAQF AISPGLTEPL LKAATEGTIP LIPGISTVSE
LMLGMDYGLK EFKFFPAEAN GGVKALQAIA GPFSQVRFCP TGGISPANYR DYLALKSVLC
IGGSWLVPAD ALEAGDYDRI TKLAREAVEG AKL</pre>
|-
!{{table heading style}} |Mol. Wt
|
22.28 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|
5.83<ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |Extinction coefficient
|
16960 - 17335 (calc based on 4 Y, 2 W, and 3 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23802.A46aa81a39903a&page=23802&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='165122'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23802.W46aa81a411220&page=23802&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='165123'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1FWR 1FWR] CRYSTAL STRUCTURE OF KDPG ALDOLASE DOUBLE MUTANT K133Q/T161K
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1FQ0 1FQ0] KDPG ALDOLASE FROM ESCHERICHIA COLI
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23802.I46aa81a46c793&page=23802&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='165124'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23802.H46aa81a5d82e8&page=23802&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='165125'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER EcoCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0A955 UniProt:P0A955]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF01081 PFAM:PF01081]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_416364 RefSeq:NP_416364]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P0A955 ModBase:P0A955]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1FQ0 PDB:1FQ0]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23802.A46aa81a641f69&page=23802&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='111656'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23802.N46a81268dd61f&page=23802&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0016052_!_carbohydrate catabolic process]][[Category:GO:0009255_!_Entner-Doudoroff pathway]][[Category:GO:0009436_!_glyoxylate catabolic process]][[Category:Complex:KDPGALDOL-4OH2OXOGLUTARALDOL-CPLX]][[Category:Products with structures in PDB]]

aspA:Gene Product(s)

2007-10-26T16:26:22Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|aspA}}{{Tab|Gene|aspA}}{{Tab On|Gene Product(s)|aspA}}{{Tab|Expression|aspA}}{{Tab|Evolution|aspA}}{{Tab|On One Page|aspA}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
AspA product
|-
!{{table heading style}} |Synonyms
|
aspartate ammonia-lyase product<ref name='LIB:Riley_2006'/>, B4139 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, AspA product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
AspA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:aspartate ammonia-lyase|aspartate ammonia-lyase]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=4.3.1.1 4.3.1.1]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28982.I46ab1fe783fe7&page=28982&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='182018'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006520
|
amino acid metabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006529
|
asparagine biosynthetic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009089
|
lysine biosynthetic process via diaminopimelate
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0008797
|
aspartate ammonia-lyase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28982.W46ab1fe993888&page=28982&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='182019'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:aspartate ammonia-lyase|aspartate ammonia-lyase]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28982.X46ab20084f4b6&page=28982&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='182020'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28982.Q46ab20099dde1&page=28982&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=ASPARTASE-MONOMER at EcoCyc]
<pre>MCLKQIIGSL KKKVHMSNNI RIEEDLLGTR EVPADAYYGV HTLRAIENFY ISNNKISDIP
EFVRGMVMVK KAAAMANKEL QTIPKSVANA IIAACDEVLN NGKCMDQFPV DVYQGGAGTS
VNMNTNEVLA NIGLELMGHQ KGEYQYLNPN DHVNKCQSTN DAYPTGFRIA VYSSLIKLVD
AINQLREGFE RKAVEFQDIL KMGRTQLQDA VPMTLGQEFR AFSILLKEEV KNIQRTAELL
LEVNLGATAI GTGLNTPKEY SPLAVKKLAE VTGFPCVPAE DLIEATSDCG AYVMVHGALK
RLAVKMSKIC NDLRLLSSGP RAGLNEINLP ELQAGSSIMP AKVNPVVPEV VNQVCFKVIG
NDTTVTMAAE AGQLQLNVME PVIGQAMFES VHILTNACYN LLEKCINGIT ANKEVCEGYV
YNSIGIVTYL NPFIGHHNGD IVGKICAETG KSVREVVLER GLLTEAELDD IFSVQNLMHP
AYKAKRYTDE SEQ</pre>
|-
!{{table heading style}} |Mol. Wt
|
52.36 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
23840 - 25340 (calc based on 16 Y, 0 W, and 12 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28982.N46ab200acd010&page=28982&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='182022'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28982.X46ab200b4fba1&page=28982&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='182023'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1JSW 1JSW] NATIVE L-ASPARTATE AMMONIA LYASE
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28982.W46ab200bb824d&page=28982&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182024'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28982.X46ab200cb4cf0&page=28982&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182025'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=ASPARTASE-MONOMER EcoCyc:ASPARTASE-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0AC38 UniProt:P0AC38]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00206 PFAM:PF00206]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_418562 RefSeq:NP_418562]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P0AC38 ModBase:P0AC38]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1JSW PDB:1JSW]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28982.Q46ab200d26c01&page=28982&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182026'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.28982.X46ab2011ab60a&page=28982&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0006520_!_amino acid metabolic process]][[Category:GO:0006529_!_asparagine biosynthetic process]][[Category:GO:0009089_!_lysine biosynthetic process via diaminopimelate]][[Category:Complex:aspartate ammonia-lyase]][[Category:Products with structures in PDB]]

mdh:Gene Product(s)

2007-10-26T16:12:07Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|mdh}}{{Tab|Gene|mdh}}{{Tab On|Gene Product(s)|mdh}}{{Tab|Expression|mdh}}{{Tab|Evolution|mdh}}{{Tab|On One Page|mdh}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
Mdh product
|-
!{{table heading style}} |Synonyms
|
malate dehydrogenase, NAD(P)-binding product<ref name='LIB:Riley_2006'/>, B3236 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Mdh product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
Mdh<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:malate dehydrogenase|malate dehydrogenase]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26920.K46aada9b03b64&page=26920&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='175126'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0016052
|
carbohydrate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006099
|
tricarboxylic acid cycle
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006113
|
fermentation
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009061
|
anaerobic respiration
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006094
|
gluconeogenesis
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009436
|
glyoxylate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0016615
|
malate dehydrogenase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26920.T46aada9c89150&page=26920&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='175127'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:malate dehydrogenase|malate dehydrogenase]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26920.Z46aadae0a13bf&page=26920&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='118000'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26920.L46a86d598a063&page=26920&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=MALATE-DEHASE-MONOMER at EcoCyc]
<pre>MKVAVLGAAG GIGQALALLL KTQLPSGSEL SLYDIAPVTP GVAVDLSHIP TAVKIKGFSG
EDATPALEGA DVVLISAGVA RKPGMDRSDL FNVNAGIVKN LVQQVAKTCP KACIGIITNP
VNTTVAIAAE VLKKAGVYDK NKLFGVTTLD IIRSNTFVAE LKGKQPGEVE VPVIGGHSGV
TILPLLSQVP GVSFTEQEVA DLTKRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR
ALQGEQGVVE CAYVEGDGQY ARFFSQPLLL GKNGVEERKS IGTLSAFEQN ALEGMLDTLK
KDIALGEEFV NK</pre>
|-
!{{table heading style}} |Mol. Wt
|
32.34 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
5960 - 6335 (calc based on 4 Y, 0 W, and 3 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26920.C46aadae3357dd&page=26920&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='175129'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26920.C46aadae3a8dbd&page=26920&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='175130'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1IE3 1IE3] CRYSTAL STRUCTURE OF R153C E. COLI MALATE DEHYDROGENASE
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1IB6 1IB6] CRYSTAL STRUCTURE OF R153C E. COLI MALATE DEHYDROGENASE
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2CMD 2CMD] THE CRYSTAL STRUCTURE OF E.COLI MALATE DEHYDROGENASE: A COMPLEX OF THE APOENZYME AND CITRATE AT 1.87 ANGSTROMS RESOLUTION
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1EMD 1EMD] CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF ESCHERICHIA COLI MALATE DEHYDROGENASE, CITRATE AND NAD AT 1.9 ANGSTROMS RESOLUTION
|

|

|-
|

|

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1CME 1CME]
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26920.Q46aadae416ce5&page=26920&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='175131'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26920.A46aadae7deecb&page=26920&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='175132'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=MALATE-DEHASE-MONOMER EcoCyc:MALATE-DEHASE-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P61889 UniProt:P61889]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00056 PFAM:PF00056]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_417703 RefSeq:NP_417703]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P61889 ModBase:P61889]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1CME PDB:1CME]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26920.Y46aadae852c44&page=26920&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='118001'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.26920.D46a86d625f9a0&page=26920&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0016052_!_carbohydrate catabolic process]][[Category:GO:0006099_!_tricarboxylic acid cycle]][[Category:GO:0006113_!_fermentation]][[Category:GO:0009061_!_anaerobic respiration]][[Category:GO:0006094_!_gluconeogenesis]][[Category:GO:0009436_!_glyoxylate catabolic process]][[Category:Complex:malate dehydrogenase]][[Category:Products with structures in PDB]]

frdD:Gene Product(s)

2007-10-24T16:48:33Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|frdD}}{{Tab|Gene|frdD}}{{Tab On|Gene Product(s)|frdD}}{{Tab|Expression|frdD}}{{Tab|Evolution|frdD}}{{Tab|On One Page|frdD}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
FrdD product
|-
!{{table heading style}} |Synonyms
|
fumarate reductase (anaerobic), membrane anchor subunit product<ref name='LIB:Riley_2006'/>, B4151 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, FrdD product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
fumarate reductase membrane protein<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:fumarate reductase|fumarate reductase]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
*
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29015.W46ab2129d83bd&page=29015&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='182158'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0009061
|
anaerobic respiration
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009054
|
electron acceptor activity
|

|

|

|
F
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006113
|
fermentation
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0000104
|
succinate dehydrogenase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29015.K46ab212b605dc&page=29015&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='182159'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:fumarate reductase|fumarate reductase]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29015.Z46ab213a75172&page=29015&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='182160'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-
|
plasma membrane
|

|

|
From EcoCyc<ref name='LIB:EcoCyc11.1'/>
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29015.V46ab213bc8ef5&page=29015&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=FUM-MEMB2 at EcoCyc]
<pre>MINPNPKRSD EPVFWGLFGA GGMWSAIIAP VMILLVGILL PLGLFPGDAL SYERVLAFAQ
SFIGRVFLFL MIVLPLWCGL HRMHHAMHDL KIHVPAGKWV FYGLAAILTV VTLIGVVTI</pre>
|-
!{{table heading style}} |Mol. Wt
|
13.11 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
24980 - 25105 (calc based on 2 Y, 4 W, and 1 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29015.H46ab213d7d3ed&page=29015&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='182162'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29015.X46ab213e02627&page=29015&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='182163'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1L0V 1L0V] Quinol-Fumarate Reductase with Menaquinol Molecules
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KFY 1KFY] QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KF6 1KF6] E. coli Quinol-Fumarate Reductase with Bound Inhibitor HQNO
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29015.S46ab213e68e0f&page=29015&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182164'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29015.Q46ab2140b0bb4&page=29015&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182165'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=FUM-MEMB2 EcoCyc:FUM-MEMB2]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0A8Q3 UniProt:P0A8Q3]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF02313 PFAM:PF02313]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_418575 RefSeq:NP_418575]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P0A8Q3 ModBase:P0A8Q3]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KF6 PDB:1KF6]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29015.L46ab2141257b8&page=29015&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182166'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29015.N46ab2145aa91a&page=29015&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0009061_!_anaerobic respiration]][[Category:GO:0009054_!_electron acceptor activity]][[Category:GO:0006113_!_fermentation]][[Category:Complex:fumarate reductase]][[Category:Location:plasma membrane]][[Category:Products with structures in PDB]]

frdC:Gene Product(s)

2007-10-24T16:47:48Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|frdC}}{{Tab|Gene|frdC}}{{Tab On|Gene Product(s)|frdC}}{{Tab|Expression|frdC}}{{Tab|Evolution|frdC}}{{Tab|On One Page|frdC}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
FrdC product
|-
!{{table heading style}} |Synonyms
|
fumarate reductase (anaerobic), membrane anchor subunit product<ref name='LIB:Riley_2006'/>, B4152 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, FrdC product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
fumarate reductase membrane protein<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:fumarate reductase|fumarate reductase]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
*
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29018.G46ab21472b80d&page=29018&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='182168'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0009061
|
anaerobic respiration
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009054
|
electron acceptor activity
|

|

|

|
F
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006113
|
fermentation
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0000104
|
succinate dehydrogenase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29018.Q46ab2148a8344&page=29018&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='182169'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:fumarate reductase|fumarate reductase]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29018.I46ab2158462c8&page=29018&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='182170'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-
|
plasma membrane
|

|

|
From EcoCyc<ref name='LIB:EcoCyc11.1'/>
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29018.N46ab2159a66cf&page=29018&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=FUM-MEMB1 at EcoCyc]
<pre>MTTKRKPYVR PMTSTWWKKL PFYRFYMLRE GTAVPAVWFS IELIFGLFAL KNGPEAWAGF
VDFLQNPVIV IINLITLAAA LLHTKTWFEL APKAANIIVK DEKMGPEPII KSLWAVTVVA
TIVILFVALY W</pre>
|-
!{{table heading style}} |Mol. Wt
|
15.02 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
44460 (calc based on 4 Y, 7 W, and 0 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29018.F46ab215b64908&page=29018&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='182172'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29018.Q46ab215bdd80d&page=29018&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='182173'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1L0V 1L0V] Quinol-Fumarate Reductase with Menaquinol Molecules
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KFY 1KFY] QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KF6 1KF6] E. coli Quinol-Fumarate Reductase with Bound Inhibitor HQNO
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29018.E46ab215c4e6d2&page=29018&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182174'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29018.E46ab215e9f37b&page=29018&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182175'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=FUM-MEMB1 EcoCyc:FUM-MEMB1]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0A8Q0 UniProt:P0A8Q0]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF02300 PFAM:PF02300]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_418576 RefSeq:NP_418576]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P0A8Q0 ModBase:P0A8Q0]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KF6 PDB:1KF6]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29018.Y46ab215f12e01&page=29018&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182176'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29018.Y46ab216395b7d&page=29018&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0009061_!_anaerobic respiration]][[Category:GO:0009054_!_electron acceptor activity]][[Category:GO:0006113_!_fermentation]][[Category:Complex:fumarate reductase]][[Category:Location:plasma membrane]][[Category:Products with structures in PDB]]

frdB:Gene Product(s)

2007-10-24T16:45:31Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|frdB}}{{Tab|Gene|frdB}}{{Tab On|Gene Product(s)|frdB}}{{Tab|Expression|frdB}}{{Tab|Evolution|frdB}}{{Tab|On One Page|frdB}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
FrdB product
|-
!{{table heading style}} |Synonyms
|
fumarate reductase (anaerobic), Fe-S subunit product<ref name='LIB:Riley_2006'/>, B4153 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, FrdB product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
fumarate reductase iron-sulfur protein<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:fumarate reductase|fumarate reductase]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29020.B46ab216531821&page=29020&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='182178'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006113
|
fermentation
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009061
|
anaerobic respiration
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009054
|
electron acceptor activity
|

|

|

|
F
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0000104
|
succinate dehydrogenase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29020.O46ab2166d1b08&page=29020&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='182179'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:fumarate reductase|fumarate reductase]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29020.I46ab21902fb6e&page=29020&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='182180'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29020.G46ab21917cb56&page=29020&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=FUM-FE-S at EcoCyc]
<pre>MAEMKNLKIE VVRYNPEVDT APHSAFYEVP YDATTSLLDA LGYIKDNLAP DLSYRWSCRM
AICGSCGMMV NNVPKLACKT FLRDYTDGMK VEALANFPIE RDLVVDMTHF IESLEAIKPY
IIGNSRTADQ GTNIQTPAQM AKYHQFSGCI NCGLCYAACP QFGLNPEFIG PAAITLAHRY
NEDSRDHGKK ERMAQLNSQN GVWSCTFVGY CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT LKPR</pre>
|-
!{{table heading style}} |Mol. Wt
|
27.12 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|
6.46<ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |Extinction coefficient
|
27390 - 28765 (calc based on 11 Y, 2 W, and 11 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29020.Q46ab2192c662c&page=29020&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='182182'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29020.W46ab21934aa32&page=29020&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='182183'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1L0V 1L0V] Quinol-Fumarate Reductase with Menaquinol Molecules
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KFY 1KFY] QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KF6 1KF6] E. coli Quinol-Fumarate Reductase with Bound Inhibitor HQNO
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29020.B46ab2193b1182&page=29020&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182184'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29020.U46ab219604b12&page=29020&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182185'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=FUM-FE-S EcoCyc:FUM-FE-S]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0AC47 UniProt:P0AC47]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00111 PFAM:PF00111]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_418577 RefSeq:NP_418577]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KF6 PDB:1KF6]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29020.H46ab219669842&page=29020&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182186'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29020.M46ab219a22235&page=29020&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0006113_!_fermentation]][[Category:GO:0009061_!_anaerobic respiration]][[Category:GO:0009054_!_electron acceptor activity]][[Category:Complex:fumarate reductase]][[Category:Products with structures in PDB]]

frdA:Gene Product(s)

2007-10-24T16:44:29Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|frdA}}{{Tab|Gene|frdA}}{{Tab On|Gene Product(s)|frdA}}{{Tab|Expression|frdA}}{{Tab|Evolution|frdA}}{{Tab|On One Page|frdA}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
FrdA product
|-
!{{table heading style}} |Synonyms
|
fumarate reductase (anaerobic) catalytic and NAD/flavoprotein subunit product<ref name='LIB:Riley_2006'/>, B4154 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, FrdA product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
fumarate reductase flavoprotein<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:fumarate reductase|fumarate reductase]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29022.X46ab219c3075b&page=29022&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='182188'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006113
|
fermentation
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009061
|
anaerobic respiration
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009054
|
electron acceptor activity
|

|

|

|
F
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009398
|
FMN biosynthetic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0000104
|
succinate dehydrogenase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29022.E46ab219db3733&page=29022&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='182189'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:fumarate reductase|fumarate reductase]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29022.X46ab21cc7351e&page=29022&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='182190'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29022.W46ab21cdbd6c0&page=29022&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=FUM-FLAVO at EcoCyc]
<pre>MQTFQADLAI VGAGGAGLRA AIAAAQANPN AKIALISKVY PMRSHTVAAE GGSAAVAQDH
DSFEYHFHDT VAGGDWLCEQ DVVDYFVHHC PTEMTQLELW GCPWSRRPDG SVNVRRFGGM
KIERTWFAAD KTGFHMLHTL FQTSLQFPQI QRFDEHFVLD ILVDDGHVRG LVAMNMMEGT
LVQIRANAVV MATGGAGRVY RYNTNGGIVT GDGMGMALSH GVPLRDMEFV QYHPTGLPGS
GILMTEGCRG EGGILVNKNG YRYLQDYGMG PETPLGEPKN KYMELGPRDK VSQAFWHEWR
KGNTISTPRG DVVYLDLRHL GEKKLHERLP FICELAKAYV GVDPVKEPIP VRPTAHYTMG
GIETDQNCET RIKGLFAVGE CSSVGLHGAN RLGSNSLAEL VVFGRLAGEQ ATERAATAGN
GNEAAIEAQA AGVEQRLKDL VNQDGGENWA KIRDEMGLAM EEGCGIYRTP ELMQKTIDKL
AELQERFKRV RITDTSSVFN TDLLYTIELG HGLNVAECMA HSAMARKESR GAHQRLDEGC
TERDDVNFLK HTLAFRDADG TTRLEYSDVK ITTLPPAKRV YGGEADAADK AEAANKKEKA NG</pre>
|-
!{{table heading style}} |Mol. Wt
|
65.97 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|
6.23<ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |Extinction coefficient
|
63830 - 65080 (calc based on 17 Y, 7 W, and 10 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29022.A46ab21cef30cd&page=29022&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='182192'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29022.E46ab21cf767ea&page=29022&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='182193'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1L0V 1L0V] Quinol-Fumarate Reductase with Menaquinol Molecules
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KFY 1KFY] QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KF6 1KF6] E. coli Quinol-Fumarate Reductase with Bound Inhibitor HQNO
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29022.U46ab21cfdac4c&page=29022&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182194'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29022.T46ab21d22c472&page=29022&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182195'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=FUM-FLAVO EcoCyc:FUM-FLAVO]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P00363 UniProt:P00363]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00890 PFAM:PF00890]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_418578 RefSeq:NP_418578]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P00363 ModBase:P00363]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KF6 PDB:1KF6]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29022.U46ab21d298704&page=29022&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='182196'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.29022.F46ab21d722f9b&page=29022&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0006113_!_fermentation]][[Category:GO:0009061_!_anaerobic respiration]][[Category:GO:0009054_!_electron acceptor activity]][[Category:GO:0009398_!_FMN biosynthetic process]][[Category:Complex:fumarate reductase]][[Category:Products with structures in PDB]]

aceF:Gene Product(s)

2007-10-24T16:42:27Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|aceF}}{{Tab|Gene|aceF}}{{Tab On|Gene Product(s)|aceF}}{{Tab|Expression|aceF}}{{Tab|Evolution|aceF}}{{Tab|On One Page|aceF}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
AceF product
|
AceF product
|-
!{{table heading style}} |Synonyms
|
pyruvate dehydrogenase, dihydrolipoyltransacetylase component E2 product<ref name='LIB:Riley_2006'/>, B0115 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|
B0115 product<ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |Product description
|
AceF-lipoate<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|
AceF-S-acetyldihydrolipoate<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12]<ref name='LIB:Riley_2006'/>
|
*
|-
|colspan='3'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19732.A46aa1ca55bfb2&page=19732&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>

====AceF-lipoate====


{|class = 'sortable' {{Prettytable}} id='152239'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0016052
|
carbohydrate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006086
|
acetyl-CoA biosynthetic process from pyruvate
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006096
|
glycolysis
|

|

|

|
P
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0009436
|
glyoxylate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009061
|
anaerobic respiration
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0004742
|
dihydrolipoyllysine-residue acetyltransferase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19732.O46aa1ca656a02&page=19732&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>

====AceF-lipoate====


{|class = 'sortable' {{Prettytable}} id='152240'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19732.C46aa1ccec9619&page=19732&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

====AceF-S-acetyldihydrolipoate====


{|class = 'sortable' {{Prettytable}} id='152240'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19732.C46aa1ccec9619&page=19732&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='100862'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19732.C46a73258c6bce&page=19732&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=ACEF-LIPOATE at EcoCyc]
<pre>MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ AGIVKEIKVS
VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP AAAAAKDVNV PDIGSDEVEV
TEILVKVGDK VEAEQSLITV EGDKASMEVP APFAGTVKEI KVNVGDKVST GSLIMVFEVA
GEAGAAAPAA KQEAAPAAAP APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT
VEGDKASMEV PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA
AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT GRKGRILRED
VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI EEVELGRIQK ISGANLSRNW
VMIPHVTHFD KTDITELEAF RKQQNEEAAK RKLDVKITPV VFIMKAVAAA LEQMPRFNSS
LSEDGQRLTL KKYINIGVAV DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA
GEMQGGCFTI SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS
FDHRVIDGAD GARFITIINN TLSDIRRLVM</pre>
|
[http://biocyc.org/ECOLI/sequence-aa?object= at EcoCyc]
<pre></pre>
|-
!{{table heading style}} |Mol. Wt
|
66.1 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|
66.1 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|

|-
!{{table heading style}} |Extinction coefficient
|
20970 - 21095 (calc based on 3 Y, 3 W, and 1 C residues)
|
0 (calc based on 0 Y, 0 W, and 0 C residues)
|-
|colspan='3'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19732.Z46aa1cd084f28&page=19732&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='152242'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19732.K46aa1cd0dccb1&page=19732&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='100863'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19732.Q46a7325a53db3&page=19732&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='152243'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19732.E46aa1cd17b26c&page=19732&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='152244'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=ACEF-LIPOATE EcoCyc:ACEF-LIPOATE]
|

|-
|
[http://swissmodel.expasy.org/repository/ SwissModel] ([[SwissModel|EcoliWiki Page]])
|
[http://swissmodel.expasy.org/repository/smr.php?job=2&sptr_ac=P06959 SwissModel:P06959]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P06959 UniProt:P06959]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?3 of PF00364 PFAM:3 of PF00364]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_414657 RefSeq:NP_414657]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P06959 ModBase:P06959]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19732.K46aa1cd1c40af&page=19732&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='100864'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19732.M46a7326586da9&page=19732&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0016052_!_carbohydrate catabolic process]][[Category:GO:0006086_!_acetyl-CoA biosynthetic process from pyruvate]][[Category:GO:0006096_!_glycolysis]][[Category:GO:0009436_!_glyoxylate catabolic process]][[Category:GO:0009061_!_anaerobic respiration]]

aceE:Gene Product(s)

2007-10-24T16:38:14Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|aceE}}{{Tab|Gene|aceE}}{{Tab On|Gene Product(s)|aceE}}{{Tab|Expression|aceE}}{{Tab|Evolution|aceE}}{{Tab|On One Page|aceE}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
AceE product
|-
!{{table heading style}} |Synonyms
|
pyruvate dehydrogenase, decarboxylase component E1, thiamin-binding product<ref name='LIB:Riley_2006'/>, B0114 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, AceE product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
subunit of E1p component of pyruvate dehydrogenase complex<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:E1P-CPLX|E1P-CPLX]]<ref name='LIB:EcoCyc10.6'/>; [[:Category:Complex:pyruvate dehydrogenase multienzyme complex|pyruvate dehydrogenase multienzyme complex]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19725.Z46aa1c77829b4&page=19725&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='152231'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0016052
|
carbohydrate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006086
|
acetyl-CoA biosynthetic process from pyruvate
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006096
|
glycolysis
|

|

|

|
P
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0009436
|
glyoxylate catabolic process
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009061
|
anaerobic respiration
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0004738
|
pyruvate dehydrogenase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19725.D46aa1c793dfc3&page=19725&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='152232'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:E1P-CPLX|E1P-CPLX]]
|
could be indirect
|-
|
Protein
|
Subunits of [[:Category:Complex:pyruvate dehydrogenase multienzyme complex|pyruvate dehydrogenase multienzyme complex]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19725.W46aa1c9bec3a0&page=19725&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='100860'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19725.R46a73228a6118&page=19725&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=E1P-MONOMER at EcoCyc]
<pre>MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY
INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV
CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH
PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK
GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD
ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL
NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH
IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ
DFGALLEEQS KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS
PNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY
SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD
PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI
EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP
LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH
HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA</pre>
|-
!{{table heading style}} |Mol. Wt
|
99.67 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|
5.76<ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |Extinction coefficient
|
123080 - 123830 (calc based on 42 Y, 11 W, and 6 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19725.O46aa1c9e744e7&page=19725&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='152234'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19725.P46aa1c9ecc69c&page=19725&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='152235'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1L8A 1L8A] E. COLI PYRUVATE DEHYDROGENASE
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1RP7 1RP7] E. COLI PYRUVATE DEHYDROGENASE INHIBITOR COMPLEX
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19725.Q46aa1c9f20b2b&page=19725&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='152236'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19725.J46aa1ca04dde5&page=19725&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='152237'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=E1P-MONOMER EcoCyc:E1P-MONOMER]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1RP7 PDB:1RP7]
|

|-
|
[http://swissmodel.expasy.org/repository/ SwissModel] ([[SwissModel|EcoliWiki Page]])
|
[http://swissmodel.expasy.org/repository/smr.php?job=2&sptr_ac=P0AFG8 SwissModel:P0AFG8]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0AFG8 UniProt:P0AFG8]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_414656 RefSeq:NP_414656]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19725.H46aa1ca096fea&page=19725&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='100861'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.19725.K46a7322dea11e&page=19725&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0016052_!_carbohydrate catabolic process]][[Category:GO:0006086_!_acetyl-CoA biosynthetic process from pyruvate]][[Category:GO:0006096_!_glycolysis]][[Category:GO:0009436_!_glyoxylate catabolic process]][[Category:GO:0009061_!_anaerobic respiration]][[Category:Complex:E1P-CPLX]][[Category:Complex:pyruvate dehydrogenase multienzyme complex]][[Category:Products with structures in PDB]]

fumC:Gene Product(s)

2007-10-24T16:33:35Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|fumC}}{{Tab|Gene|fumC}}{{Tab On|Gene Product(s)|fumC}}{{Tab|Expression|fumC}}{{Tab|Evolution|fumC}}{{Tab|On One Page|fumC}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
FumC product
|-
!{{table heading style}} |Synonyms
|
fumarate hydratase (fumarase C),aerobic Class II product<ref name='LIB:Riley_2006'/>, B1611 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, FumC product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
fumarase C monomer<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:fumarase C|fumarase C]]<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=4.2.1.2 4.2.1.2]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23244.C46aa71c320a18&page=23244&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='163226'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0006099
|
tricarboxylic acid cycle
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0006113
|
fermentation
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009061
|
anaerobic respiration
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0004333
|
fumarate hydratase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23244.G46aa71c47fc24&page=23244&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='163227'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:fumarase C|fumarase C]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23244.T46aa71ded2c70&page=23244&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='110349'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23244.L46a803f117b26&page=23244&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=FUMC-MONOMER at EcoCyc]
<pre>MNTVRSEKDS MGAIDVPADK LWGAQTQRSL EHFRISTEKM PTSLIHALAL TKRAAAKVNE
DLGLLSEEKA SAIRQAADEV LAGQHDDEFP LAIWQTGSGT QSNMNMNEVL ANRASELLGG
VRGMERKVHP NDDVNKSQSS NDVFPTAMHV AALLALRKQL IPQLKTLTQT LNEKSRAFAD
IVKIGRTHLQ DATPLTLGQE ISGWVAMLEH NLKHIEYSLP HVAELALGGT AVGTGLNTHP
EYARRVADEL AVITCAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS
GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EALTMLCCQV MGNDVAINMG GASGNFELNV
FRPMVIHNFL QSVRLLADGM ESFNKHCAVG IEPNRERINQ LLNESLMLVT ALNTHIGYDK
AAEIAKKAHK EGLTLKAAAL ALGYLSEAEF DSWVRPEQMV GSMKAGR</pre>
|-
!{{table heading style}} |Mol. Wt
|
50.49 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|
6.51<ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |Extinction coefficient
|
33460 - 34335 (calc based on 4 Y, 5 W, and 7 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23244.S46aa71e26222c&page=23244&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='163229'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23244.A46aa71e2c7a05&page=23244&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='163230'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2FUS 2FUS] MUTATIONS OF FUMARASE THAT DISTINGUISH BETWEEN THE ACTIVE SITE AND A NEARBY DICARBOXYLIC ACID BINDING SITE
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KQ7 1KQ7] E315Q Mutant Form of Fumarase C from E.coli
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1FUR 1FUR] FUMARASE MUTANT H188N WITH BOUND SUBSTRATE L-MALATE AT PUTATIVE ACTIVATOR SITE
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1FUQ 1FUQ] FUMARASE WITH BOUND PYROMELLITIC ACID
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1FUP 1FUP] FUMARASE WITH BOUND PYROMELLITIC ACID
|

|

|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1FUO 1FUO] FUMARASE C WITH BOUND CITRATE
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23244.T46aa71e32aeb7&page=23244&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='163231'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23244.B46aa71e7555a7&page=23244&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='163232'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=FUMC-MONOMER EcoCyc:FUMC-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P05042 UniProt:P05042]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00206 PFAM:PF00206]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_416128 RefSeq:NP_416128]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P05042 ModBase:P05042]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1FUO PDB:1FUO]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23244.R46aa71e7aa3c9&page=23244&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='110350'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23244.T46a803fbbb6f9&page=23244&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0006099_!_tricarboxylic acid cycle]][[Category:GO:0006113_!_fermentation]][[Category:GO:0009061_!_anaerobic respiration]][[Category:Complex:fumarase C]][[Category:Products with structures in PDB]]

sdhD:Gene Product(s)

2007-10-24T16:31:22Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|sdhD}}{{Tab|Gene|sdhD}}{{Tab On|Gene Product(s)|sdhD}}{{Tab|Expression|sdhD}}{{Tab|Evolution|sdhD}}{{Tab|On One Page|sdhD}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
SdhD product
|-
!{{table heading style}} |Synonyms
|
succinate dehydrogenase, membrane subunit, binds cytochrome b556 product<ref name='LIB:Riley_2006'/>, B0722 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, DhsD product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, SdhD product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, CybS product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, small subunit of cytochrome b556 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
succinate dehydrogenase membrane protein<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:membrane-bound subcomplex of succinate dehydrogenase|membrane-bound subcomplex of succinate dehydrogenase]]<ref name='LIB:EcoCyc11.1'/>; [[:Category:Complex:succinate dehydrogenase|succinate dehydrogenase]]<ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
*
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21201.M46aa3f60a9cf4&page=21201&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='156630'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0006099
|
tricarboxylic acid cycle
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009053
|
electron donor activity
|

|

|

|
F
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0017004
|
cytochrome complex assembly
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009060
|
aerobic respiration
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0000104
|
succinate dehydrogenase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21201.N46aa3f6271c46&page=21201&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='156631'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:membrane-bound subcomplex of succinate dehydrogenase|membrane-bound subcomplex of succinate dehydrogenase]]
|
could be indirect
|-
|
Protein
|
Subunits of [[:Category:Complex:succinate dehydrogenase|succinate dehydrogenase]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21201.K46aa3f6fbd85b&page=21201&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='156632'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-
|
plasma membrane
|

|

|
From EcoCyc<ref name='LIB:EcoCyc11.1'/>
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21201.G46aa3f713f8af&page=21201&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=SDH-MEMB2 at EcoCyc]
<pre>MVSNASALGR NGVHDFILVR ATAIVLTLYI IYMVGFFATS GELTYEVWIG FFASAFTKVF
TLLALFSILI HAWIGMWQVL TDYVKPLALR LMLQLVIVVA LVVYVIYGFV VVWGV</pre>
|-
!{{table heading style}} |Mol. Wt
|
12.87 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
30940 (calc based on 6 Y, 4 W, and 0 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21201.V46aa3f72a8ad5&page=21201&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='156634'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21201.J46aa3f730f449&page=21201&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='156635'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1NEN 1NEN] Complex II (Succinate Dehydrogenase) From E. Coli with Dinitrophenol-17 inhibitor co-crystallized at the ubiquinone binding site
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21201.W46aa3f735a1eb&page=21201&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='156636'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21201.L46aa3f7419ba0&page=21201&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='156637'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=SDH-MEMB2 EcoCyc:SDH-MEMB2]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0AC44 UniProt:P0AC44]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_415250 RefSeq:NP_415250]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P0AC44 ModBase:P0AC44]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1NEN PDB:1NEN]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21201.I46aa3f74651a7&page=21201&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='105575'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21201.O46a7d12451c44&page=21201&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0006099_!_tricarboxylic acid cycle]][[Category:GO:0009053_!_electron donor activity]][[Category:GO:0017004_!_cytochrome complex assembly]][[Category:GO:0009060_!_aerobic respiration]][[Category:Complex:membrane-bound subcomplex of succinate dehydrogenase]][[Category:Complex:succinate dehydrogenase]][[Category:Location:plasma membrane]][[Category:Products with structures in PDB]]

sdhC:Gene Product(s)

2007-10-24T16:30:41Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|sdhC}}{{Tab|Gene|sdhC}}{{Tab On|Gene Product(s)|sdhC}}{{Tab|Expression|sdhC}}{{Tab|Evolution|sdhC}}{{Tab|On One Page|sdhC}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
SdhC product
|-
!{{table heading style}} |Synonyms
|
succinate dehydrogenase, membrane subunit, binds cytochrome b556 product<ref name='LIB:Riley_2006'/>, B0721 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, DhsC product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, CybA product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, SdhC product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, large subunit of cytochrome b556 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, CybL product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
succinate dehydrogenase membrane protein<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:membrane-bound subcomplex of succinate dehydrogenase|membrane-bound subcomplex of succinate dehydrogenase]]<ref name='LIB:EcoCyc11.1'/>; [[:Category:Complex:succinate dehydrogenase|succinate dehydrogenase]]<ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
*
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21197.E46aa3f47d44c4&page=21197&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='156621'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0006099
|
tricarboxylic acid cycle
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009053
|
electron donor activity
|

|

|

|
F
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0017004
|
cytochrome complex assembly
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009060
|
aerobic respiration
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0000104
|
succinate dehydrogenase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21197.M46aa3f49a9b5d&page=21197&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='156622'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:membrane-bound subcomplex of succinate dehydrogenase|membrane-bound subcomplex of succinate dehydrogenase]]
|
could be indirect
|-
|
Protein
|
Subunits of [[:Category:Complex:succinate dehydrogenase|succinate dehydrogenase]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21197.E46aa3f570537d&page=21197&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='156623'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-
|
plasma membrane
|

|

|
From EcoCyc<ref name='LIB:EcoCyc11.1'/>
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21197.X46aa3f587b47b&page=21197&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=SDH-MEMB1 at EcoCyc]
<pre>MIRNVKKQRP VNLDLQTIRF PITAIASILH RVSGVITFVA VGILLWLLGT SLSSPEGFEQ
ASAIMGSFFV KFIMWGILTA LAYHVVVGIR HMMMDFGYLE ETFEAGKRSA KISFVITVVL
SLLAGVLVW</pre>
|-
!{{table heading style}} |Mol. Wt
|
14.3 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
19480 (calc based on 2 Y, 3 W, and 0 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21197.X46aa3f59e40de&page=21197&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='156625'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21197.U46aa3f5a4a97e&page=21197&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='156626'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1NEN 1NEN] Complex II (Succinate Dehydrogenase) From E. Coli with Dinitrophenol-17 inhibitor co-crystallized at the ubiquinone binding site
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21197.C46aa3f5a95577&page=21197&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='156627'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21197.M46aa3f5b549da&page=21197&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='156628'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=SDH-MEMB1 EcoCyc:SDH-MEMB1]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P69054 UniProt:P69054]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF01127 PFAM:PF01127]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_415249 RefSeq:NP_415249]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P69054 ModBase:P69054]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1NEN PDB:1NEN]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21197.L46aa3f5ba01a1&page=21197&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='105567'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21197.Z46a7d10c8433b&page=21197&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0006099_!_tricarboxylic acid cycle]][[Category:GO:0009053_!_electron donor activity]][[Category:GO:0017004_!_cytochrome complex assembly]][[Category:GO:0009060_!_aerobic respiration]][[Category:Complex:membrane-bound subcomplex of succinate dehydrogenase]][[Category:Complex:succinate dehydrogenase]][[Category:Location:plasma membrane]][[Category:Products with structures in PDB]]

sdhB:Gene Product(s)

2007-10-24T16:29:27Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|sdhB}}{{Tab|Gene|sdhB}}{{Tab On|Gene Product(s)|sdhB}}{{Tab|Expression|sdhB}}{{Tab|Evolution|sdhB}}{{Tab|On One Page|sdhB}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
SdhB product
|-
!{{table heading style}} |Synonyms
|
succinate dehydrogenase, FeS subunit product<ref name='LIB:Riley_2006'/>, B0724 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, DhsB product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, SdhB product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
succinate dehydrogenase iron-sulfur protein<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:catalytic subcomplex of succinate dehydrogenase|catalytic subcomplex of succinate dehydrogenase]]<ref name='LIB:EcoCyc11.1'/>; [[:Category:Complex:succinate dehydrogenase|succinate dehydrogenase]]<ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21206.V46aa3f98824b5&page=21206&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='156648'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0006099
|
tricarboxylic acid cycle
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009060
|
aerobic respiration
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009053
|
electron donor activity
|

|

|

|
F
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0000104
|
succinate dehydrogenase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21206.L46aa3f9a41b97&page=21206&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='156649'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:catalytic subcomplex of succinate dehydrogenase|catalytic subcomplex of succinate dehydrogenase]]
|
could be indirect
|-
|
Protein
|
Subunits of [[:Category:Complex:succinate dehydrogenase|succinate dehydrogenase]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21206.U46aa3fadda64d&page=21206&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='156650'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-
|
plasma membrane
|

|

|
From EcoCyc<ref name='LIB:EcoCyc11.1'/>
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21206.C46aa3faf5d961&page=21206&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=SDH-FE-S at EcoCyc]
<pre>MRLEFSIYRY NPDVDDAPRM QDYTLEADEG RDMMLLDALI QLKEKDPSLS FRRSCREGVC
GSDGLNMNGK NGLACITPIS ALNQPGKKIV IRPLPGLPVI RDLVVDMGQF YAQYEKIKPY
LLNNGQNPPA REHLQMPEQR EKLDGLYECI LCACCSTSCP SFWWNPDKFI GPAGLLAAYR
FLIDSRDTET DSRLDGLSDA FSVFRCHSIM NCVSVCPKGL NPTRAIGHIK SMLLQRNA</pre>
|-
!{{table heading style}} |Mol. Wt
|
26.77 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|

|-
!{{table heading style}} |Extinction coefficient
|
22920 - 24295 (calc based on 8 Y, 2 W, and 11 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21206.P46aa3fb13dd80&page=21206&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='156652'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21206.G46aa3fb198ee7&page=21206&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='156653'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1NEN 1NEN] Complex II (Succinate Dehydrogenase) From E. Coli with Dinitrophenol-17 inhibitor co-crystallized at the ubiquinone binding site
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21206.G46aa3fb1e485c&page=21206&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='156654'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21206.N46aa3fb2a4e56&page=21206&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='156655'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=SDH-FE-S EcoCyc:SDH-FE-S]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P07014 UniProt:P07014]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_415252 RefSeq:NP_415252]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P07014 ModBase:P07014]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1NEN PDB:1NEN]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21206.E46aa3fb2f0297&page=21206&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='105594'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21206.U46a7d16272288&page=21206&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0006099_!_tricarboxylic acid cycle]][[Category:GO:0009060_!_aerobic respiration]][[Category:GO:0009053_!_electron donor activity]][[Category:Complex:catalytic subcomplex of succinate dehydrogenase]][[Category:Complex:succinate dehydrogenase]][[Category:Location:cytoplasm]][[Category:Location:plasma membrane]][[Category:Products with structures in PDB]]

sdhA:Gene Product(s)

2007-10-24T16:28:06Z

Michelle: edited by Michelle via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|sdhA}}{{Tab|Gene|sdhA}}{{Tab On|Gene Product(s)|sdhA}}{{Tab|Expression|sdhA}}{{Tab|Evolution|sdhA}}{{Tab|On One Page|sdhA}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Structure|Structure]]
|{{Sub}}[[#Gene Product Resources|Resources]]
|{{Sub}}[[#Accessions in Other Databases |Accessions]]
|{{Sub}}[[#Links |Links]]
|{{Sub}}[[#References| References]]
|{{Sub}}[[Talk:{{PAGENAMEE}}| Suggestions]]
|}
</noinclude>
==Nomenclature==


{|{{Prettytable}}
|-
!{{table heading style}} |Standard name
|
SdhA product
|-
!{{table heading style}} |Synonyms
|
succinate dehydrogenase, flavoprotein subunit product<ref name='LIB:Riley_2006'/>, B0723 product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, DhsA product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, SdhA product<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!{{table heading style}} |Product description
|
succinate dehydrogenase flavoprotein<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;

Component of ; [[:Category:Complex:catalytic subcomplex of succinate dehydrogenase|catalytic subcomplex of succinate dehydrogenase]]<ref name='LIB:EcoCyc11.1'/>; [[:Category:Complex:succinate dehydrogenase|succinate dehydrogenase]]<ref name='LIB:EcoCyc11.1'/>

|-
!{{table heading style}} |EC number (for enzymes)
|
** [http://www.brenda.uni-koeln.de/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1]<ref name='LIB:Riley_2006'/>
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21203.A46aa3f78b4a64&page=21203&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_nomenclature_help}}
<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big>


{|class = 'sortable' {{Prettytable}} id='156639'
|- {{table_heading_style}}
!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

|
C
|
Seeded from Riley et al 2006 <ref name='LIB:Riley_2006'/>.
|
required fields missing
|-
|

|
GO:0006099
|
tricarboxylic acid cycle
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009060
|
aerobic respiration
|

|

|

|
P
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0009053
|
electron donor activity
|

|

|

|
F
|
Seeded from EcoCyc 11.1<ref name='LIB:EcoCyc11.1'/>.
|
required fields missing
|-
|

|
GO:0000104
|
succinate dehydrogenase activity
|

|

|

|
F
|

|
required field missing
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21203.B46aa3f7a775d0&page=21203&pagename={{FULLPAGENAMEE}} edit table] || || || || || || || ||
|}

{{Product_GO_help}}

<big>'''Interactions'''</big>


{|class = 'sortable' {{Prettytable}} id='156640'
|- {{table heading style}}
!Partner Type!!Partner!!Notes
|-
|
Protein
|
Subunits of [[:Category:Complex:catalytic subcomplex of succinate dehydrogenase|catalytic subcomplex of succinate dehydrogenase]]
|
could be indirect
|-
|
Protein
|
Subunits of [[:Category:Complex:succinate dehydrogenase|succinate dehydrogenase]]
|
could be indirect
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21203.H46aa3f8e27b47&page=21203&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_interactions_help}}
</protect>
===Notes===

==Localization==


{|class = 'sortable' {{Prettytable}} id='156641'
|- {{table heading style}}
!Compartment!!Description!!Evidence!!Notes
|-
|
plasma membrane
|

|

|
From EcoCyc<ref name='LIB:EcoCyc11.1'/>
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21203.Q46aa3f8f9dfc7&page=21203&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_localization_help}}
<protect></protect>

===Notes===

==Structure and Physical Properties==
{{BacktoTop}}
<protect>
<big>'''Physical Properties'''</big>


{|{{Prettytable}}
|-
!{{table heading style}} |Sequence
|
[http://biocyc.org/ECOLI/sequence-aa?object=SDH-FLAVO at EcoCyc]
<pre>MKLPVREFDA VVIGAGGAGM RAALQISQSG QTCALLSKVF PTRSHTVSAQ GGITVALGNT
HEDNWEWHMY DTVKGSDYIG DQDAIEYMCK TGPEAILELE HMGLPFSRLD DGRIYQRPFG
GQSKNFGGEQ AARTAAAADR TGHALLHTLY QQNLKNHTTI FSEWYALDLV KNQDGAVVGC
TALCIETGEV VYFKARATVL ATGGAGRIYQ STTNAHINTG DGVGMAIRAG VPVQDMEMWQ
FHPTGIAGAG VLVTEGCRGE GGYLLNKHGE RFMERYAPNA KDLAGRDVVA RSIMIEIREG
RGCDGPWGPH AKLKLDHLGK EVLESRLPGI LELSRTFAHV DPVKEPIPVI PTCHYMMGGI
PTKVTGQALT VNEKGEDVVV PGLFAVGEIA CVSVHGANRL GGNSLLDLVV FGRAAGLHLQ
ESIAEQGALR DASESDVEAS LDRLNRWNNN RNGEDPVAIR KALQECMQHN FSVFREGDAM
AKGLEQLKVI RERLKNARLD DTSSEFNTQR VECLELDNLM ETAYATAVSA NFRTESRGAH
SRFDFPDRDD ENWLCHSLYL PESESMTRRS VNMEPKLRPA FPPKIRTY</pre>
|-
!{{table heading style}} |Mol. Wt
|
64.42 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |pI
|
6.21<ref name='LIB:EcoCyc10.6'/>
|-
!{{table heading style}} |Extinction coefficient
|
59360 - 60735 (calc based on 14 Y, 7 W, and 11 C residues)
|-
|colspan='2'|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21203.N46aa3f918dbb7&page=21203&pagename={{FULLPAGENAMEE}} edit table]
|}

{{Product_physical_properties_help}}

<big>'''Domains/Motifs/Modification Sites'''</big>


{|class = 'sortable' {{Prettytable}} id='156643'
|- {{table heading style}}
!Type!!Residues!!Description!!Notes
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21203.T46aa3f91e8b5d&page=21203&pagename={{FULLPAGENAMEE}} edit table] || || ||
|}

{{Product_domains_motifs_help}}

<big>'''Structure'''</big>


{|class = 'sortable' {{Prettytable}} id='156644'
|- {{table heading style}}
!Structure Type!!Organism!!Accession!!Residues covered!!Notes
|-
|
X-RAY DIFFRACTION

|
Escherichia coli

|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1NEN 1NEN] Complex II (Succinate Dehydrogenase) From E. Coli with Dinitrophenol-17 inhibitor co-crystallized at the ubiquinone binding site
|

|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21203.H46aa3f923f8d2&page=21203&pagename={{FULLPAGENAMEE}} edit table] || || || ||
|}

{{Product_structure_help}}
</protect>
===Notes===

==Gene Product Resources==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='156645'
|- {{table_heading_style}}
!Resource type!!Source!!Notes/Reference
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21203.H46aa3f92f32f9&page=21203&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_resources_help}}
<protect></protect>
===Notes===

==Accessions in Other Databases==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='156646'
|- {{table_heading_style}}
!Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=SDH-FLAVO EcoCyc:SDH-FLAVO]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[http://www.expasy.ch/cgi-bin/sprot-search-ac?P0AC41 UniProt:P0AC41]
|

|-
|
[http://www.sanger.ac.uk/Software/Pfam/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00890 PFAM:PF00890]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_415251 RefSeq:NP_415251]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P0AC41 ModBase:P0AC41]
|

|-
|
[http://www.rcsb.org/pdb PDB] ([[PDB|EcoliWiki Page]])
|
[http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1NEN PDB:1NEN]
|

|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21203.I46aa3f934a7b9&page=21203&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Product_accessions_help}}
<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' {{Prettytable}} id='105584'
|- {{table_heading_style}}
!Name!!URL!!Comments
|-class='sortbottom'
|[{{SERVER}}/colipedia/index.php?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.21203.S46a7d14407490&page=21203&pagename={{FULLPAGENAMEE}} edit table] || ||
|}

{{Links_help}}

<noinclude>
==References==
{{BacktoTop}}
{{RefHelp}}
<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0006099_!_tricarboxylic acid cycle]][[Category:GO:0009060_!_aerobic respiration]][[Category:GO:0009053_!_electron donor activity]][[Category:Complex:catalytic subcomplex of succinate dehydrogenase]][[Category:Complex:succinate dehydrogenase]][[Category:Location:cytoplasm]][[Category:Location:plasma membrane]][[Category:Products with structures in PDB]]