EcoliWiki - User contributions [en]

mutS:Quickview

2009-05-05T15:48:26Z

M gehrig2000: /* Notes */

recQ:Quickview

2009-04-16T17:08:02Z

M gehrig2000: /* Notes */

recQ:Quickview

2009-04-16T16:52:56Z

M gehrig2000: /* Notes */

recQ:Quickview

2009-04-16T16:51:26Z

M gehrig2000: /* Notes */

add:Quickview

2009-03-12T16:22:28Z

M gehrig2000: /* Notes */

PMID:15498720

2009-03-12T16:21:53Z

M gehrig2000: Fill PMID: Page!

{{RightTOC}}

 '''Aiuti, A''' (2004) Gene therapy for adenosine-deaminase-deficient severe combined immunodeficiency.''Best Pract Res Clin Haematol'' '''17''':505-16

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>Adenosine-deaminase-deficient SCID was the first inherited disease to be treated with gene therapy. This life-threatening disorder is characterized by a purine defect that leads to impaired immune functions, recurrent infections and systemic metabolic abnormalities. The early gene therapy trials showed the safety and feasibility of engineering haematopoietic stem cells and peripheral blood lymphocytes using retroviral vectors. However, all patients were maintained on enzyme-replacement therapy, which prevented the evaluation of its efficacy and abolished the selective advantage for gene-corrected cells. It is only recently that the clinical efficacy of gene therapy has been investigated in the absence of enzyme-replacement therapy. Results of these studies showed that gene therapy with peripheral blood lymphocytes allowed correction of the T-cell defect, but provided insufficient systemic detoxification. Gene transfer in bone marrow stem cells, associated with non-myeloablative conditioning, allowed full immunological and metabolic correction of the adenosine-deaminase defect with clinical benefit. These results have important implications for future applications of gene therapy in other blood-borne disorders.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15498720 PubMed] Online version:[http://dx.doi.org/10.1016/j.beha.2004.05.012 10.1016/j.beha.2004.05.012]
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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

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

{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.150112.F49b936a0bf897&page=150112&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:15498720

2009-03-12T16:21:52Z

M gehrig2000: New PMID: Page!

add:Quickview

2009-03-12T16:20:11Z

M gehrig2000: /* References */

add:Quickview

2009-03-12T16:19:49Z

M gehrig2000: /* Notes */

add:Quickview

2009-03-12T16:18:06Z

M gehrig2000: /* References */

add:Quickview

2009-03-12T16:15:32Z

M gehrig2000: /* Notes */

add:Gene Product(s)

2009-03-05T18:12:21Z

M gehrig2000: Table edited by M gehrig2000 via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|add}}{{Tab|Gene|add}}{{Tab On|Gene Product(s)|add}}{{Tab|Expression|add}}{{Tab|Evolution|add}}{{Tab|On One Page|add}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Domains/Motifs/Modification Sites|Domains]]
|{{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==

{{Product_nomenclature_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Standard name
||
Add
|-
!align=left {{table heading style}} |Synonyms
||
adenosine deaminase<ref name='LIB:Riley_2006'/>, B1623<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Add<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!align=left {{table heading style}} |Product description
||

Adenosine deaminase; mutants affect growth on deoxyadenosine in purA, B mutants<ref name='LIB:EcoGene'/>
|-
!align=left {{table heading style}} |EC number (for enzymes)
||
* [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4]<ref name='LIB:Riley_2006'/>

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.U46aa72e0944f5&page=23273&pagename={{FULLPAGENAMEE}}&type=1&template=Product_nomenclature_table edit table] ||
|}


<protect></protect>
===Notes===

Adenosine deaminase is the enzyme that catalyzes the irreversible deamination of adenosine or deoxyadenosine to inosine or deoxyinosine. The active site of ADA contains residues of a Histidine, 2 Aspartic acids, one Glutamic acid, and a zinc atom. The overall mechanism involves a hydroxyl group addition to C6 of adenosine, which forms the tetrahedral transition state intermediate. Then, the ammonia elimination forms inosine. Zinc acts as a powerful electrophile, which allows a water molecule to attack C6. Glutamic acid interacts with N1 and donates a proton, reducing the N1=C6 double bond character, allowing the hydroxyl nucleophilic attack. A Histidine residue and the carboxylic group of aspartic acid stabilizes and orients the zinc-bound water molecule. The ammonia elimination pathway is not quite understood but is the final step in the mechanism of adenosine deaminase.

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big> 
{{Product_GO_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0016787
|
hydrolase activity
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0378
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0009168
|
purine ribonucleoside monophosphate biosynthetic process
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000002 GO_REF:0000020
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR001365 InterPro:IPR006330 InterPro:IPR006650 HAMAP:MF_00540
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0009117
|
nucleotide metabolic process
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0546
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0004000
|
adenosine deaminase activity
|
GO_REF:0000002 GO_REF:0000003 GO_REF:0000020
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR006330 EC:3.5.4.4 HAMAP:MF_00540
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0019239
|
deaminase activity
|
GO_REF:0000002 GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR001365 InterPro:IPR006650
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

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

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

|

|

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

|
GO:0004000
|
adenosine deaminase activity
|
PMID:4874315
|
IDA: Inferred from Direct Assay
|

|
F
|

|
complete
|-
|

|
GO:0005488
|
binding
|
PMID:3486673
|
ISS: Inferred from Sequence or Structural Similarity
|
UniProtKB:P56658
|
F
|
CHEBI:27834 (Deoxycoformycin mechanistically inhibits Add).
|
complete
|-
|

|
GO:0004000
|
adenosine deaminase activity
|
PMID:5335916
|
IDA: Inferred from Direct Assay
|

|
F
|

|
complete
|-
|

|
GO:0004000
|
adenosine deaminase activity
|
PMID:765747
|
IMP: Inferred from Mutant Phenotype
|

|
F
|

|
complete

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.N46aa72e194b25&page=23273&pagename={{FULLPAGENAMEE}}&type=&template=GO_table_product edit table] || || || || || || || ||
|}


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

{{Product_interactions_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Partner Type!!Partner!!Notes!!References!!Evidence
|-
|
Protein
|
rpsM 
|

|
PMID:16606699
|
Experiment(s):EBI-1140315 
|-
|
Protein
|
arpA 
|

|
PMID:16606699
|
Experiment(s):EBI-1140315 
|-
|
Protein
|
rplT 
|

|
PMID:16606699
|
Experiment(s):EBI-1140315 
|-
|
Protein
|
insC1 
|

|
PMID:16606699
|
Experiment(s):EBI-1140315 
|-
|
Protein
|
ligA 
|

|
PMID:16606699
|
Experiment(s):EBI-1140315 
|-
|
Protein
|
gcd 
|

|
PMID:16606699
|
Experiment(s):EBI-1140315 
|-
|
Small Molecule
|
CHEBI:27834 (Deoxycoformycin)
|
Inhibitor of Add activity
|

|

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.H46aa72e958e91&page=23273&pagename={{FULLPAGENAMEE}}&type=&template=Product_interactions_table edit table] || || || ||
|}


</protect>
===Notes===

==Localization==

{{Product_localization_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Compartment!!Description!!Evidence!!Notes

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.L46a805074c1b0&page=23273&pagename={{FULLPAGENAMEE}}&type=&template=Product_localization_table edit table] || || ||
|}


<protect></protect>

===Notes===

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

{{Product_physical_properties_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Sequence
||
[http://biocyc.org/ECOLI/sequence-aa?object=ADENODEAMIN-MONOMER at EcoCyc]
<pre>MIDTTLPLTD IHRHLDGNIR PQTILELGRQ YNISLPAQSL ETLIPHVQVI ANEPDLVSFL
TKLDWGVKVL ASLDACRRVA FENIEDAARH GLHYVELRFS PGYMAMAHQL PVAGVVEAVI
DGVREGCRTF GVQAKLIGIM SRTFGEAACQ QELEAFLAHR DQITALDLAG DELGFPGSLF
LSHFNRARDA GWHITVHAGE AAGPESIWQA IRELGAERIG HGVKAIEDRA LMDFLAEQQI
GIESCLTSNI QTSTVAELAA HPLKTFLEHG IRASINTDDP GVQGVDIIHE YTVAAPAAGL
SREQIRQAQI NGLEMAFLSA EEKRALREKV AAK</pre>
|-
!align=left {{table heading style}} |Mol. Wt
||
36.4 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!align=left {{table heading style}} |pI
||
5.63<ref name='LIB:EcoCyc10.6'/>
|-
!align=left {{table heading style}} |Extinction coefficient
||
22460 - 22960 (calc based on 4 Y, 3 W, and 4 C residues)

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.V46aa72eb37ca8&page=23273&pagename={{FULLPAGENAMEE}}&type=1&template=Product_phys_prop_table edit table] ||
|}


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

{{Product_domains_motifs_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Type!!Residues!!Description!!Notes

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.M46aa72eb9d42b&page=23273&pagename={{FULLPAGENAMEE}}&type=&template=Product_motif_table edit table] || || ||
|}


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

{{Product_structure_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Structures
||
<beststructure>add
562</beststructure>

|-
!align=left {{table heading style}} |Models
||

View models at:
* [http://dragon.bio.purdue.edu/ecolpredict2/localsearch/cgi-bin/search3.cgi?q=add&sub=keywordSearc EcoliPredict]
* [http://modbase.compbio.ucsf.edu/modbase-cgi/model_search.cgi?searchmode=default&displaymode=moddetail&searchproperties=ALL&searchvalue=add&organism=562&organismtext= ModBase]
* [http://bioinf.cs.ucl.ac.uk/psipred/ PSI-PRED]
* [http://www.ebi.ac.uk/msd-srv/pqs/ Protein Quaternary Structure] (PQS)
* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.H46a80508dcdd8&page=23273&pagename={{FULLPAGENAMEE}}&type=1&template=Product_structure_table edit table] ||
|}


</protect>
===Notes===

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

{{Product_resources_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Resource type!!Source!!Notes/Reference

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.U46aa72ec59068&page=23273&pagename={{FULLPAGENAMEE}}&type=&template=Product_resource_table edit table] || ||
|}


<protect></protect>
===Notes===

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

{{Gene_accessions_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=ADENODEAMIN-MONOMER EcoCyc:ADENODEAMIN-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[[uniprot:P22333|UniProt:P22333]]
|

|-
|
[http://pfam.sanger.ac.uk/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://pfam.sanger.ac.uk/family?acc=PF00962 PFAM:PF00962]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_416140 RefSeq:NP_416140]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P22333 ModBase:P22333]
|

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.C46aa72ecb0698&page=23273&pagename={{FULLPAGENAMEE}}&type=0&template=Gene_accessions_table edit table] || ||
|}


<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Name!!URL!!Comments

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.F46a8050c4b2e7&page=23273&pagename={{FULLPAGENAMEE}}&type=0&template=Links_table edit table] || ||
|}


<noinclude>
==References==
{{BacktoTop}}

<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0015949_!_nucleobase, nucleoside and nucleotide interconversion]]

PMID:5335916

2009-02-24T18:10:47Z

M gehrig2000: /* Significance {{HelpIcon|Help:Literature}} */

{{RightTOC}}

 '''Wolfenden, R, Sharpless, TK and Allan, R''' (1967) Substrate binding by adenosine deaminase. Specificity, pH dependence, and competition by mercurials.''J. Biol. Chem.'' '''242''':977-83

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>No abstract in PubMed</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=5335916 PubMed] 
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

After purification of Ada, there was found to be no complicating metal or cofactor requirements, a broad pH activity range, and also a broad substrate specificity. The enzyme functioned within the pH ranges of 2.7 to 9.5 in .1M glycine buffers, and was insensitive to the concentration of the buffer. The Mercury atom proved to be a competitive inhibitor in mammalian Ada.

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

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

{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Add
|

|
GO:0004000
|
adenosine deaminase activity
|
ISS: Inferred from Sequence or Structural Similarity
|
UniProtKB:P56658
|
F
|
Seen in Figure 3, adenosine deaminase was irreversibly inactive below pKa 3.7 and above pKa 8.9. Also, in Figure 4, a reciprocal graph shows the rate of deamination of adenosine in the presence of different concentrations of mersalyl acid, a mercurial diuretic. The graph clearly shows a decrease in activity of Ada with increasing amounts of mersalyl acid.
|
complete

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.148921.G490fa08594c6c&page=148921&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

==References==

<references/>

Category:GO:0004000 ! adenosine deaminase activity

2009-02-24T18:09:23Z

M gehrig2000: New GO term category page

PMID:5335916

2009-02-24T18:05:47Z

M gehrig2000: Table edited by M gehrig2000 via TableEdit

{{RightTOC}}

 '''Wolfenden, R, Sharpless, TK and Allan, R''' (1967) Substrate binding by adenosine deaminase. Specificity, pH dependence, and competition by mercurials.''J. Biol. Chem.'' '''242''':977-83

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>No abstract in PubMed</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=5335916 PubMed] 
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

After purification of ADA, there was found to be no complicating metal or cofactor requirements, a broad pH activity range, and also a broad substrate specificity. The enzyme functioned within the pH ranges of 2.7 to 9.5 in .1M glycine buffers, and was insensitive to the concentration of the buffer. The Mercury atom proved to be a competitive inhibitor in mammalian ADA.

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

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

{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Add
|

|
GO:0004000
|
adenosine deaminase activity
|
ISS: Inferred from Sequence or Structural Similarity
|
UniProtKB:P56658
|
F
|
Seen in Figure 3, adenosine deaminase was irreversibly inactive below pKa 3.7 and above pKa 8.9. Also, in Figure 4, a reciprocal graph shows the rate of deamination of adenosine in the presence of different concentrations of mersalyl acid, a mercurial diuretic. The graph clearly shows a decrease in activity of Ada with increasing amounts of mersalyl acid.
|
complete

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.148921.G490fa08594c6c&page=148921&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

==References==

<references/>

PMID:5335916

2009-02-24T17:55:36Z

M gehrig2000: /* Significance {{HelpIcon|Help:Literature}} */

{{RightTOC}}

 '''Wolfenden, R, Sharpless, TK and Allan, R''' (1967) Substrate binding by adenosine deaminase. Specificity, pH dependence, and competition by mercurials.''J. Biol. Chem.'' '''242''':977-83

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>No abstract in PubMed</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=5335916 PubMed] 
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

After purification of ADA, there was found to be no complicating metal or cofactor requirements, a broad pH activity range, and also a broad substrate specificity. The enzyme functioned within the pH ranges of 2.7 to 9.5 in .1M glycine buffers, and was insensitive to the concentration of the buffer. The Mercury atom proved to be a competitive inhibitor in mammalian ADA.

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

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

{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
Add
|

|
GO:0004000
|
adenosine deaminase activity
|
ISS: Inferred from Sequence or Structural Similarity
|
UniProtKB:P56658
|
F
|

|
complete

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.148921.G490fa08594c6c&page=148921&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

==References==

<references/>

ada:Gene Product(s)

2009-02-24T17:51:54Z

M gehrig2000: Table edited by M gehrig2000 via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|ada}}{{Tab|Gene|ada}}{{Tab On|Gene Product(s)|ada}}{{Tab|Expression|ada}}{{Tab|Evolution|ada}}{{Tab|On One Page|ada}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Domains/Motifs/Modification Sites|Domains]]
|{{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==

{{Product_nomenclature_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Standard name
||
Ada
|-
!align=left {{table heading style}} |Synonyms
||
fused DNA-binding transcriptional dual regulator<ref name='LIB:Riley_2006'/>, O6-methylguanine-DNA methyltransferase<ref name='LIB:Riley_2006'/>, B2213<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Ada<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!align=left {{table heading style}} |Product description
||
Ada transcriptional dual regulator<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!align=left {{table heading style}} |EC number (for enzymes)
||
** [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.63 2.1.1.63]<ref name='LIB:Riley_2006'/>

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.W46aa98c9b8d17&page=24595&pagename={{FULLPAGENAMEE}}&type=1&template=Product_nomenclature_table edit table] ||
|}


<protect></protect>
===Notes===

Adenosine deaminase is the enzyme that catalyzes the irreversible deamination of adenosine or deoxyadenosine to inosine or deoxyinosine. The active site of ADA contains residues of a Histidine, 2 Aspartic acids, one Glutamic acid, and a zinc atom. The overall mechanism involves a hydroxyl group addition to C6 of adenosine, which forms the tetrahedral transition state intermediate. Then, the ammonia elimination forms inosine. Zinc acts as a powerful electrophile, which allows a water molecule to attack C6. Glutamic acid interacts with N1 and donates a proton, reducing the N1=C6 double bond character, allowing the hydroxyl nucleophilic attack. A Histidine residue and the carboxylic group of aspartic acid stabilizes and orients the zinc-bound water molecule. The ammonia elimination pathway is not quite understood but is the final step in the mechanism of adenosine deaminase.

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big> 
{{Product_GO_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005622
|
intracellular
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005
|
C
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003908
|
methylated-DNA-(protein)-cysteine S-methyltransferase activity
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000003
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR001497 InterPro:IPR008332 EC:2.1.1.63
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003677
|
DNA binding
|
GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR004026 SP_KW:KW-0238
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003700
|
transcription factor activity
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003824
|
catalytic activity
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR014048
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0046872
|
metal ion binding
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0479
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0016740
|
transferase activity
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0808
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0043565
|
sequence-specific DNA binding
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006281
|
DNA repair
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000002 GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR001497 InterPro:IPR004026 InterPro:IPR008332 InterPro:IPR014048 SP_KW:KW-0234
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006350
|
transcription
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0804
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006355
|
regulation of transcription, DNA-dependent
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005 InterPro:IPR004026 SP_KW:KW-0805
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006974
|
response to DNA damage stimulus
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0227
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0008168
|
methyltransferase activity
|
GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR004026 SP_KW:KW-0489
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0008270
|
zinc ion binding
|
GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR004026 SP_KW:KW-0862
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

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

|
GO:0016563
|
transcription activator activity
|

|

|

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

|
GO:0016564
|
transcription repressor activity
|

|

|

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

|
GO:0004000
|
adenosine deaminase activity
|
PMID:5335916
|
IDA: Inferred from Direct Assay
|

|
F
|

|
complete

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.Z46aa98cac84ca&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=GO_table_product edit table] || || || || || || || ||
|}


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

{{Product_interactions_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Partner Type!!Partner!!Notes!!References!!Evidence
|-
|
Protein
|
rplB 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
rpsC 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
moeB 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
fur 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
rpsG 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
ybiA 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.G46aa98ec716d5&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_interactions_table edit table] || || || ||
|}


</protect>
===Notes===

==Localization==

{{Product_localization_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Compartment!!Description!!Evidence!!Notes
|-
|
membrane
|

|

|
From EcoCyc<ref name='LIB:EcoCyc11.1'/>

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.U46aa98ed35ea6&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_localization_table edit table] || || ||
|}


<protect></protect>

===Notes===

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

{{Product_physical_properties_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Sequence
||
[http://biocyc.org/ECOLI/sequence-aa?object=PD00230 at EcoCyc]
<pre>MKKATCLTDD QRWQSVLARD PNADGEFVFA VRTTGIFCRP SCRARHALRE NVSFYANASE
ALAAGFRPCK RCQPEKANAQ QHRLDKITHA CRLLEQETPV TLEALADQVA MSPFHLHRLF
KATTGMTPKA WQQAWRARRL RESLAKGESV TTSILNAGFP DSSSYYRKAD ETLGMTAKQF
RHGGENLAVR YALADCELGR CLVAESERGI CAILLGDDDA TLISELQQMF PAADNAPADL
MFQQHVREVI ASLNQRDTPL TLPLDIRGTA FQQQVWQALR TIPCGETVSY QQLANAIGKP
KAVRAVASAC AANKLAIIIP CHRVVRGDGT LSGYRWGVSR KAQLLRREAE NEER</pre>
|-
!align=left {{table heading style}} |Mol. Wt
||
39.32 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!align=left {{table heading style}} |pI
||
8.69<ref name='LIB:EcoCyc10.6'/>
|-
!align=left {{table heading style}} |Extinction coefficient
||
36440 - 37940 (calc based on 6 Y, 5 W, and 12 C residues)

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.N46aa98eec4384&page=24595&pagename={{FULLPAGENAMEE}}&type=1&template=Product_phys_prop_table edit table] ||
|}


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

{{Product_domains_motifs_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Type!!Residues!!Description!!Notes

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.Z46aa98ef3d7e3&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_motif_table edit table] || || ||
|}


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

{{Product_structure_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Structures
||
<beststructure>ada
562</beststructure>

|-
!align=left {{table heading style}} |Models
||

View models at:
* [http://dragon.bio.purdue.edu/ecolpredict2/localsearch/cgi-bin/search3.cgi?q=ada&sub=keywordSearc EcoliPredict]
* [http://modbase.compbio.ucsf.edu/modbase-cgi/model_search.cgi?searchmode=default&displaymode=moddetail&searchproperties=ALL&searchvalue=ada&organism=562&organismtext= ModBase]
* [http://bioinf.cs.ucl.ac.uk/psipred/ PSI-PRED]
* [http://www.ebi.ac.uk/msd-srv/pqs/ Protein Quaternary Structure] (PQS)
* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.M46a82cf901614&page=24595&pagename={{FULLPAGENAMEE}}&type=1&template=Product_structure_table edit table] ||
|}


</protect>
===Notes===

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

{{Product_resources_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Resource type!!Source!!Notes/Reference

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.K46aa98f0046e8&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_resource_table edit table] || ||
|}


<protect></protect>
===Notes===

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

{{Gene_accessions_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=PD00230 EcoCyc:PD00230]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[[uniprot:P06134|UniProt:P06134]]
|

|-
|
[http://pfam.sanger.ac.uk/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://pfam.sanger.ac.uk/family?acc=PF02805 PFAM:PF02805]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_416717 RefSeq:NP_416717]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P06134 ModBase:P06134]
|

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.L46aa98f06149e&page=24595&pagename={{FULLPAGENAMEE}}&type=0&template=Gene_accessions_table edit table] || ||
|}


<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Name!!URL!!Comments

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.A46a82cfd89960&page=24595&pagename={{FULLPAGENAMEE}}&type=0&template=Links_table edit table] || ||
|}


<noinclude>
==References==
{{BacktoTop}}

<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0006281_!_DNA repair]][[Category:GO:0006350_!_transcription]][[Category:GO:0016563_!_transcription activator activity]][[Category:GO:0016564_!_transcription repressor activity]][[Category:Location:membrane]]

ada:Gene Product(s)

2009-02-19T18:16:29Z

M gehrig2000: /* Notes */

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|ada}}{{Tab|Gene|ada}}{{Tab On|Gene Product(s)|ada}}{{Tab|Expression|ada}}{{Tab|Evolution|ada}}{{Tab|On One Page|ada}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Domains/Motifs/Modification Sites|Domains]]
|{{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==

{{Product_nomenclature_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Standard name
||
Ada
|-
!align=left {{table heading style}} |Synonyms
||
fused DNA-binding transcriptional dual regulator<ref name='LIB:Riley_2006'/>, O6-methylguanine-DNA methyltransferase<ref name='LIB:Riley_2006'/>, B2213<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Ada<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!align=left {{table heading style}} |Product description
||
Ada transcriptional dual regulator<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!align=left {{table heading style}} |EC number (for enzymes)
||
** [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.63 2.1.1.63]<ref name='LIB:Riley_2006'/>

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.W46aa98c9b8d17&page=24595&pagename={{FULLPAGENAMEE}}&type=1&template=Product_nomenclature_table edit table] ||
|}


<protect></protect>
===Notes===

Adenosine deaminase is the enzyme that catalyzes the irreversible deamination of adenosine or deoxyadenosine to inosine or deoxyinosine. The active site of ADA contains residues of a Histidine, 2 Aspartic acids, one Glutamic acid, and a zinc atom. The overall mechanism involves a hydroxyl group addition to C6 of adenosine, which forms the tetrahedral transition state intermediate. Then, the ammonia elimination forms inosine. Zinc acts as a powerful electrophile, which allows a water molecule to attack C6. Glutamic acid interacts with N1 and donates a proton, reducing the N1=C6 double bond character, allowing the hydroxyl nucleophilic attack. A Histidine residue and the carboxylic group of aspartic acid stabilizes and orients the zinc-bound water molecule. The ammonia elimination pathway is not quite understood but is the final step in the mechanism of adenosine deaminase.

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big> 
{{Product_GO_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005622
|
intracellular
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005
|
C
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003908
|
methylated-DNA-(protein)-cysteine S-methyltransferase activity
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000003
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR001497 InterPro:IPR008332 EC:2.1.1.63
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003677
|
DNA binding
|
GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR004026 SP_KW:KW-0238
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003700
|
transcription factor activity
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003824
|
catalytic activity
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR014048
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0046872
|
metal ion binding
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0479
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0016740
|
transferase activity
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0808
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0043565
|
sequence-specific DNA binding
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006281
|
DNA repair
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000002 GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR001497 InterPro:IPR004026 InterPro:IPR008332 InterPro:IPR014048 SP_KW:KW-0234
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006350
|
transcription
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0804
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006355
|
regulation of transcription, DNA-dependent
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005 InterPro:IPR004026 SP_KW:KW-0805
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006974
|
response to DNA damage stimulus
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0227
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0008168
|
methyltransferase activity
|
GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR004026 SP_KW:KW-0489
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0008270
|
zinc ion binding
|
GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR004026 SP_KW:KW-0862
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

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

|
GO:0016563
|
transcription activator activity
|

|

|

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

|
GO:0016564
|
transcription repressor activity
|

|

|

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

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.Z46aa98cac84ca&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=GO_table_product edit table] || || || || || || || ||
|}


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

{{Product_interactions_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Partner Type!!Partner!!Notes!!References!!Evidence
|-
|
Protein
|
rplB 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
rpsC 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
moeB 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
fur 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
rpsG 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
ybiA 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.G46aa98ec716d5&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_interactions_table edit table] || || || ||
|}


</protect>
===Notes===

==Localization==

{{Product_localization_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Compartment!!Description!!Evidence!!Notes
|-
|
membrane
|

|

|
From EcoCyc<ref name='LIB:EcoCyc11.1'/>

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.U46aa98ed35ea6&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_localization_table edit table] || || ||
|}


<protect></protect>

===Notes===

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

{{Product_physical_properties_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Sequence
||
[http://biocyc.org/ECOLI/sequence-aa?object=PD00230 at EcoCyc]
<pre>MKKATCLTDD QRWQSVLARD PNADGEFVFA VRTTGIFCRP SCRARHALRE NVSFYANASE
ALAAGFRPCK RCQPEKANAQ QHRLDKITHA CRLLEQETPV TLEALADQVA MSPFHLHRLF
KATTGMTPKA WQQAWRARRL RESLAKGESV TTSILNAGFP DSSSYYRKAD ETLGMTAKQF
RHGGENLAVR YALADCELGR CLVAESERGI CAILLGDDDA TLISELQQMF PAADNAPADL
MFQQHVREVI ASLNQRDTPL TLPLDIRGTA FQQQVWQALR TIPCGETVSY QQLANAIGKP
KAVRAVASAC AANKLAIIIP CHRVVRGDGT LSGYRWGVSR KAQLLRREAE NEER</pre>
|-
!align=left {{table heading style}} |Mol. Wt
||
39.32 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!align=left {{table heading style}} |pI
||
8.69<ref name='LIB:EcoCyc10.6'/>
|-
!align=left {{table heading style}} |Extinction coefficient
||
36440 - 37940 (calc based on 6 Y, 5 W, and 12 C residues)

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.N46aa98eec4384&page=24595&pagename={{FULLPAGENAMEE}}&type=1&template=Product_phys_prop_table edit table] ||
|}


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

{{Product_domains_motifs_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Type!!Residues!!Description!!Notes

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.Z46aa98ef3d7e3&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_motif_table edit table] || || ||
|}


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

{{Product_structure_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Structures
||
<beststructure>ada
562</beststructure>

|-
!align=left {{table heading style}} |Models
||

View models at:
* [http://dragon.bio.purdue.edu/ecolpredict2/localsearch/cgi-bin/search3.cgi?q=ada&sub=keywordSearc EcoliPredict]
* [http://modbase.compbio.ucsf.edu/modbase-cgi/model_search.cgi?searchmode=default&displaymode=moddetail&searchproperties=ALL&searchvalue=ada&organism=562&organismtext= ModBase]
* [http://bioinf.cs.ucl.ac.uk/psipred/ PSI-PRED]
* [http://www.ebi.ac.uk/msd-srv/pqs/ Protein Quaternary Structure] (PQS)
* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.M46a82cf901614&page=24595&pagename={{FULLPAGENAMEE}}&type=1&template=Product_structure_table edit table] ||
|}


</protect>
===Notes===

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

{{Product_resources_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Resource type!!Source!!Notes/Reference

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.K46aa98f0046e8&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_resource_table edit table] || ||
|}


<protect></protect>
===Notes===

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

{{Gene_accessions_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=PD00230 EcoCyc:PD00230]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[[uniprot:P06134|UniProt:P06134]]
|

|-
|
[http://pfam.sanger.ac.uk/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://pfam.sanger.ac.uk/family?acc=PF02805 PFAM:PF02805]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_416717 RefSeq:NP_416717]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P06134 ModBase:P06134]
|

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.L46aa98f06149e&page=24595&pagename={{FULLPAGENAMEE}}&type=0&template=Gene_accessions_table edit table] || ||
|}


<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Name!!URL!!Comments

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.A46a82cfd89960&page=24595&pagename={{FULLPAGENAMEE}}&type=0&template=Links_table edit table] || ||
|}


<noinclude>
==References==
{{BacktoTop}}

<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0006281_!_DNA repair]][[Category:GO:0006350_!_transcription]][[Category:GO:0016563_!_transcription activator activity]][[Category:GO:0016564_!_transcription repressor activity]][[Category:Location:membrane]]

ada:Gene Product(s)

2009-02-19T18:12:06Z

M gehrig2000: /* Notes */

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|ada}}{{Tab|Gene|ada}}{{Tab On|Gene Product(s)|ada}}{{Tab|Expression|ada}}{{Tab|Evolution|ada}}{{Tab|On One Page|ada}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Domains/Motifs/Modification Sites|Domains]]
|{{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==

{{Product_nomenclature_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Standard name
||
Ada
|-
!align=left {{table heading style}} |Synonyms
||
fused DNA-binding transcriptional dual regulator<ref name='LIB:Riley_2006'/>, O6-methylguanine-DNA methyltransferase<ref name='LIB:Riley_2006'/>, B2213<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Ada<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!align=left {{table heading style}} |Product description
||
Ada transcriptional dual regulator<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!align=left {{table heading style}} |EC number (for enzymes)
||
** [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.63 2.1.1.63]<ref name='LIB:Riley_2006'/>

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.W46aa98c9b8d17&page=24595&pagename={{FULLPAGENAMEE}}&type=1&template=Product_nomenclature_table edit table] ||
|}


<protect></protect>
===Notes===

Adenosine deaminase is the irreversible deamination of adenosine or deoxyadenosine to inosine or deoxyinosine. The active site of ADA contains residues of a Histidine, 2 Aspartic acids, one Glutamic acid, and a zinc atom. The overall mechanism involves a hydroxyl group addition to C6 of adenosine, which forms the tetrahedral transition state intermediate. Then, the ammonia elimination forms inosine. Zinc acts as a powerful electrophile, which allows a water molecule to attack C6. Glutamic acid interacts with N1 and donates a proton, reducing the N1=C6 double bond character, allowing the hydroxyl nucleophilic attack. A Histidine residue and the carboxylic group of aspartic acid stabilizes and orients the zinc-bound water molecule. The ammonia elimination pathway is not quite understood but is the final step in the mechanism of adenosine deaminase.

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big> 
{{Product_GO_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005622
|
intracellular
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005
|
C
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003908
|
methylated-DNA-(protein)-cysteine S-methyltransferase activity
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000003
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR001497 InterPro:IPR008332 EC:2.1.1.63
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003677
|
DNA binding
|
GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR004026 SP_KW:KW-0238
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003700
|
transcription factor activity
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003824
|
catalytic activity
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR014048
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0046872
|
metal ion binding
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0479
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0016740
|
transferase activity
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0808
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0043565
|
sequence-specific DNA binding
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006281
|
DNA repair
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000002 GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR001497 InterPro:IPR004026 InterPro:IPR008332 InterPro:IPR014048 SP_KW:KW-0234
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006350
|
transcription
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0804
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006355
|
regulation of transcription, DNA-dependent
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005 InterPro:IPR004026 SP_KW:KW-0805
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006974
|
response to DNA damage stimulus
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0227
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0008168
|
methyltransferase activity
|
GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR004026 SP_KW:KW-0489
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0008270
|
zinc ion binding
|
GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR004026 SP_KW:KW-0862
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

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

|
GO:0016563
|
transcription activator activity
|

|

|

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

|
GO:0016564
|
transcription repressor activity
|

|

|

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

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.Z46aa98cac84ca&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=GO_table_product edit table] || || || || || || || ||
|}


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

{{Product_interactions_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Partner Type!!Partner!!Notes!!References!!Evidence
|-
|
Protein
|
rplB 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
rpsC 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
moeB 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
fur 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
rpsG 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
ybiA 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.G46aa98ec716d5&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_interactions_table edit table] || || || ||
|}


</protect>
===Notes===

==Localization==

{{Product_localization_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Compartment!!Description!!Evidence!!Notes
|-
|
membrane
|

|

|
From EcoCyc<ref name='LIB:EcoCyc11.1'/>

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.U46aa98ed35ea6&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_localization_table edit table] || || ||
|}


<protect></protect>

===Notes===

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

{{Product_physical_properties_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Sequence
||
[http://biocyc.org/ECOLI/sequence-aa?object=PD00230 at EcoCyc]
<pre>MKKATCLTDD QRWQSVLARD PNADGEFVFA VRTTGIFCRP SCRARHALRE NVSFYANASE
ALAAGFRPCK RCQPEKANAQ QHRLDKITHA CRLLEQETPV TLEALADQVA MSPFHLHRLF
KATTGMTPKA WQQAWRARRL RESLAKGESV TTSILNAGFP DSSSYYRKAD ETLGMTAKQF
RHGGENLAVR YALADCELGR CLVAESERGI CAILLGDDDA TLISELQQMF PAADNAPADL
MFQQHVREVI ASLNQRDTPL TLPLDIRGTA FQQQVWQALR TIPCGETVSY QQLANAIGKP
KAVRAVASAC AANKLAIIIP CHRVVRGDGT LSGYRWGVSR KAQLLRREAE NEER</pre>
|-
!align=left {{table heading style}} |Mol. Wt
||
39.32 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!align=left {{table heading style}} |pI
||
8.69<ref name='LIB:EcoCyc10.6'/>
|-
!align=left {{table heading style}} |Extinction coefficient
||
36440 - 37940 (calc based on 6 Y, 5 W, and 12 C residues)

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.N46aa98eec4384&page=24595&pagename={{FULLPAGENAMEE}}&type=1&template=Product_phys_prop_table edit table] ||
|}


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

{{Product_domains_motifs_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Type!!Residues!!Description!!Notes

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.Z46aa98ef3d7e3&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_motif_table edit table] || || ||
|}


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

{{Product_structure_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Structures
||
<beststructure>ada
562</beststructure>

|-
!align=left {{table heading style}} |Models
||

View models at:
* [http://dragon.bio.purdue.edu/ecolpredict2/localsearch/cgi-bin/search3.cgi?q=ada&sub=keywordSearc EcoliPredict]
* [http://modbase.compbio.ucsf.edu/modbase-cgi/model_search.cgi?searchmode=default&displaymode=moddetail&searchproperties=ALL&searchvalue=ada&organism=562&organismtext= ModBase]
* [http://bioinf.cs.ucl.ac.uk/psipred/ PSI-PRED]
* [http://www.ebi.ac.uk/msd-srv/pqs/ Protein Quaternary Structure] (PQS)
* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.M46a82cf901614&page=24595&pagename={{FULLPAGENAMEE}}&type=1&template=Product_structure_table edit table] ||
|}


</protect>
===Notes===

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

{{Product_resources_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Resource type!!Source!!Notes/Reference

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.K46aa98f0046e8&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_resource_table edit table] || ||
|}


<protect></protect>
===Notes===

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

{{Gene_accessions_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=PD00230 EcoCyc:PD00230]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[[uniprot:P06134|UniProt:P06134]]
|

|-
|
[http://pfam.sanger.ac.uk/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://pfam.sanger.ac.uk/family?acc=PF02805 PFAM:PF02805]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_416717 RefSeq:NP_416717]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P06134 ModBase:P06134]
|

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.L46aa98f06149e&page=24595&pagename={{FULLPAGENAMEE}}&type=0&template=Gene_accessions_table edit table] || ||
|}


<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Name!!URL!!Comments

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.A46a82cfd89960&page=24595&pagename={{FULLPAGENAMEE}}&type=0&template=Links_table edit table] || ||
|}


<noinclude>
==References==
{{BacktoTop}}

<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0006281_!_DNA repair]][[Category:GO:0006350_!_transcription]][[Category:GO:0016563_!_transcription activator activity]][[Category:GO:0016564_!_transcription repressor activity]][[Category:Location:membrane]]

ada:Gene Product(s)

2009-02-19T18:10:01Z

M gehrig2000: /* Notes */

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|ada}}{{Tab|Gene|ada}}{{Tab On|Gene Product(s)|ada}}{{Tab|Expression|ada}}{{Tab|Evolution|ada}}{{Tab|On One Page|ada}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Domains/Motifs/Modification Sites|Domains]]
|{{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==

{{Product_nomenclature_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Standard name
||
Ada
|-
!align=left {{table heading style}} |Synonyms
||
fused DNA-binding transcriptional dual regulator<ref name='LIB:Riley_2006'/>, O6-methylguanine-DNA methyltransferase<ref name='LIB:Riley_2006'/>, B2213<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Ada<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!align=left {{table heading style}} |Product description
||
Ada transcriptional dual regulator<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!align=left {{table heading style}} |EC number (for enzymes)
||
** [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.63 2.1.1.63]<ref name='LIB:Riley_2006'/>

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.W46aa98c9b8d17&page=24595&pagename={{FULLPAGENAMEE}}&type=1&template=Product_nomenclature_table edit table] ||
|}


<protect></protect>
===Notes===

Adenosine deaminase is the irreversible deamination of adenosine or deoxyadenosine to inosine or deoxyinosine. The active site of ADA contains residues of a Histidine, 2 Aspartic acids, one Glutamic acid, and a zinc atom. The overall mechanism involves a hydroxyl group addition to C6 of adenosine, which forms the tetrahedral transition state intermediate. Then, the ammonia elimination forms inosine. Zinc acts as a powerful electrophile, which allows a water molecule to attack C6. Glutamic acid interacts with N1 and donates a proton, reducing the N1=C6 double bond character, allowing the hydroxyl nucleophilic attack. A Histidine residue and the carboxylic group of aspartic acid stabilizes and orients the zinc-bound water molecule. The ammonia elimination is not quite understood but is the final step in the mechanism of adenosine deaminase.

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big> 
{{Product_GO_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0005622
|
intracellular
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005
|
C
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003908
|
methylated-DNA-(protein)-cysteine S-methyltransferase activity
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000003
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR001497 InterPro:IPR008332 EC:2.1.1.63
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003677
|
DNA binding
|
GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR004026 SP_KW:KW-0238
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003700
|
transcription factor activity
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0003824
|
catalytic activity
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR014048
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0046872
|
metal ion binding
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0479
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0016740
|
transferase activity
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0808
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0043565
|
sequence-specific DNA binding
|
GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006281
|
DNA repair
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000002 GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR001497 InterPro:IPR004026 InterPro:IPR008332 InterPro:IPR014048 SP_KW:KW-0234
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006350
|
transcription
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0804
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006355
|
regulation of transcription, DNA-dependent
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR000005 InterPro:IPR004026 SP_KW:KW-0805
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0006974
|
response to DNA damage stimulus
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0227
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0008168
|
methyltransferase activity
|
GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR004026 SP_KW:KW-0489
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0008270
|
zinc ion binding
|
GO_REF:0000002 GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR004026 SP_KW:KW-0862
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

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

|
GO:0016563
|
transcription activator activity
|

|

|

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

|
GO:0016564
|
transcription repressor activity
|

|

|

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

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.Z46aa98cac84ca&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=GO_table_product edit table] || || || || || || || ||
|}


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

{{Product_interactions_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Partner Type!!Partner!!Notes!!References!!Evidence
|-
|
Protein
|
rplB 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
rpsC 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
moeB 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
fur 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
rpsG 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 
|-
|
Protein
|
ybiA 
|

|
PMID:16606699
|
Experiment(s):EBI-1142195 

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.G46aa98ec716d5&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_interactions_table edit table] || || || ||
|}


</protect>
===Notes===

==Localization==

{{Product_localization_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Compartment!!Description!!Evidence!!Notes
|-
|
membrane
|

|

|
From EcoCyc<ref name='LIB:EcoCyc11.1'/>

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.U46aa98ed35ea6&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_localization_table edit table] || || ||
|}


<protect></protect>

===Notes===

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

{{Product_physical_properties_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Sequence
||
[http://biocyc.org/ECOLI/sequence-aa?object=PD00230 at EcoCyc]
<pre>MKKATCLTDD QRWQSVLARD PNADGEFVFA VRTTGIFCRP SCRARHALRE NVSFYANASE
ALAAGFRPCK RCQPEKANAQ QHRLDKITHA CRLLEQETPV TLEALADQVA MSPFHLHRLF
KATTGMTPKA WQQAWRARRL RESLAKGESV TTSILNAGFP DSSSYYRKAD ETLGMTAKQF
RHGGENLAVR YALADCELGR CLVAESERGI CAILLGDDDA TLISELQQMF PAADNAPADL
MFQQHVREVI ASLNQRDTPL TLPLDIRGTA FQQQVWQALR TIPCGETVSY QQLANAIGKP
KAVRAVASAC AANKLAIIIP CHRVVRGDGT LSGYRWGVSR KAQLLRREAE NEER</pre>
|-
!align=left {{table heading style}} |Mol. Wt
||
39.32 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!align=left {{table heading style}} |pI
||
8.69<ref name='LIB:EcoCyc10.6'/>
|-
!align=left {{table heading style}} |Extinction coefficient
||
36440 - 37940 (calc based on 6 Y, 5 W, and 12 C residues)

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.N46aa98eec4384&page=24595&pagename={{FULLPAGENAMEE}}&type=1&template=Product_phys_prop_table edit table] ||
|}


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

{{Product_domains_motifs_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Type!!Residues!!Description!!Notes

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.Z46aa98ef3d7e3&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_motif_table edit table] || || ||
|}


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

{{Product_structure_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Structures
||
<beststructure>ada
562</beststructure>

|-
!align=left {{table heading style}} |Models
||

View models at:
* [http://dragon.bio.purdue.edu/ecolpredict2/localsearch/cgi-bin/search3.cgi?q=ada&sub=keywordSearc EcoliPredict]
* [http://modbase.compbio.ucsf.edu/modbase-cgi/model_search.cgi?searchmode=default&displaymode=moddetail&searchproperties=ALL&searchvalue=ada&organism=562&organismtext= ModBase]
* [http://bioinf.cs.ucl.ac.uk/psipred/ PSI-PRED]
* [http://www.ebi.ac.uk/msd-srv/pqs/ Protein Quaternary Structure] (PQS)
* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.M46a82cf901614&page=24595&pagename={{FULLPAGENAMEE}}&type=1&template=Product_structure_table edit table] ||
|}


</protect>
===Notes===

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

{{Product_resources_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Resource type!!Source!!Notes/Reference

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.K46aa98f0046e8&page=24595&pagename={{FULLPAGENAMEE}}&type=&template=Product_resource_table edit table] || ||
|}


<protect></protect>
===Notes===

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

{{Gene_accessions_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=PD00230 EcoCyc:PD00230]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[[uniprot:P06134|UniProt:P06134]]
|

|-
|
[http://pfam.sanger.ac.uk/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://pfam.sanger.ac.uk/family?acc=PF02805 PFAM:PF02805]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_416717 RefSeq:NP_416717]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P06134 ModBase:P06134]
|

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.L46aa98f06149e&page=24595&pagename={{FULLPAGENAMEE}}&type=0&template=Gene_accessions_table edit table] || ||
|}


<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Name!!URL!!Comments

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.24595.A46a82cfd89960&page=24595&pagename={{FULLPAGENAMEE}}&type=0&template=Links_table edit table] || ||
|}


<noinclude>
==References==
{{BacktoTop}}

<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0006281_!_DNA repair]][[Category:GO:0006350_!_transcription]][[Category:GO:0016563_!_transcription activator activity]][[Category:GO:0016564_!_transcription repressor activity]][[Category:Location:membrane]]

PMID:4874315

2009-02-17T18:03:33Z

M gehrig2000: Table edited by M gehrig2000 via TableEdit

{{RightTOC}}

 '''Remy, CN and Love, SH''' (1968) Induction of adenosine deaminase in Escherichia coli.''J. Bacteriol.'' '''96''':76-85

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>Supplementing the salts-glucose medium of Escherichia coli with adenine initiates induction of adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4), growth inhibition, and an increased potential for the net deamination of adenine. The extent and duration of these events are proportional to the initial adenine concentration and are dependent upon adenylate pyrophosphorylase and repression of histidine biosynthesis for maximal expression. The conversion of adenine to hypoxanthine, though limited in rate, occurs concurrently with induction and accounts for the progressively decreasing rate of deaminase induction, since hypoxanthine is a relatively ineffective inducer. The subsequent decrease in deaminase activity is due to dilution by continued cell division and by enzyme inactivation which occurs during the late-log and early-stationary phases. The partially purified deaminase is labile to a number of environmental conditions, particularly to phosphate buffers of pH 6.8 or less. A disproportionately slow rate of adenine deamination by cells utilizing lactate permits a more prolonged period of induction and, consequently, a greater quantity of enzyme to be synthesized; cell division, but not enzyme inactivation, reduces enzyme concentration. The adenosine deaminases of Aerobacter aerogenes and Salmonella typhimurium are not inducible.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4874315 PubMed] 
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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

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

{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|
[[add:Gene_Product(s)]]
|

|
GO:0004000
|
adenosine deaminase activity
|
IDA: Inferred from Direct Assay
|

|
F
|
As shown in Table 2, the specific activity of Add is .086 in the presence of 2 mM adenine with the unit of enzyme activity defined as the amount of enzyme that converts 1 umol of deoxyadenosine to 1 umol of deoxyinosine per minute.
|
complete

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.149987.K499af9bf1079f&page=149987&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:4874315

2009-02-17T17:54:07Z

M gehrig2000: Fill PMID: Page!

{{RightTOC}}

 '''Remy, CN and Love, SH''' (1968) Induction of adenosine deaminase in Escherichia coli.''J. Bacteriol.'' '''96''':76-85

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || <protect>Supplementing the salts-glucose medium of Escherichia coli with adenine initiates induction of adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4), growth inhibition, and an increased potential for the net deamination of adenine. The extent and duration of these events are proportional to the initial adenine concentration and are dependent upon adenylate pyrophosphorylase and repression of histidine biosynthesis for maximal expression. The conversion of adenine to hypoxanthine, though limited in rate, occurs concurrently with induction and accounts for the progressively decreasing rate of deaminase induction, since hypoxanthine is a relatively ineffective inducer. The subsequent decrease in deaminase activity is due to dilution by continued cell division and by enzyme inactivation which occurs during the late-log and early-stationary phases. The partially purified deaminase is labile to a number of environmental conditions, particularly to phosphate buffers of pH 6.8 or less. A disproportionately slow rate of adenine deamination by cells utilizing lactate permits a more prolonged period of induction and, consequently, a greater quantity of enzyme to be synthesized; cell division, but not enzyme inactivation, reduces enzyme concentration. The adenosine deaminases of Aerobacter aerogenes and Salmonella typhimurium are not inducible.</protect>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4874315 PubMed] 
|}

==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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

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

{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.149987.K499af9bf1079f&page=149987&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table] || || || || || || || ||
|}
</protect>

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

==See also==

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

PMID:4874315

2009-02-17T17:54:06Z

M gehrig2000: New PMID: Page!

add:Gene Product(s)

2009-02-17T17:53:43Z

M gehrig2000: Table edited by M gehrig2000 via TableEdit

{{#css:Suppresslinks.css}}<css>{{:Suppresslinks.css}}</css>
<noinclude>{{TabsTop}}
{{Tab|Quickview|add}}{{Tab|Gene|add}}{{Tab On|Gene Product(s)|add}}{{Tab|Expression|add}}{{Tab|Evolution|add}}{{Tab|On One Page|add}}{{TabsBottom}}
{|
|-
|{{Sub}}[[#Nomenclature |Nomenclature]]
|{{Sub}}[[#Function |Function]]
|{{Sub}}[[#Interactions |Interactions]]
|{{Sub}}[[#Localization |Localization]]
|{{Sub}}[[#Sequence|Sequence]]
|{{Sub}}[[#Domains/Motifs/Modification Sites|Domains]]
|{{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==

{{Product_nomenclature_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Standard name
||
Add
|-
!align=left {{table heading style}} |Synonyms
||
adenosine deaminase<ref name='LIB:Riley_2006'/>, B1623<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Add<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>
|-
!align=left {{table heading style}} |Product description
||
ADENODEAMIN<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>

|-
!align=left {{table heading style}} |EC number (for enzymes)
||
** [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4]<ref name='LIB:Riley_2006'/>

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.U46aa72e0944f5&page=23273&pagename={{FULLPAGENAMEE}}&type=1&template=Product_nomenclature_table edit table] ||
|}


<protect></protect>
===Notes===

==Function==
{{BacktoTop}}
<protect>
<big>'''Gene Ontology'''</big> 
{{Product_GO_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
|-
|

|
GO:0016787
|
hydrolase activity
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0378
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0009168
|
purine ribonucleoside monophosphate biosynthetic process
|
GO_REF:0000002 GO_REF:0000002 GO_REF:0000002 GO_REF:0000020
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR001365 InterPro:IPR006330 InterPro:IPR006650 HAMAP:MF_00540
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0009117
|
nucleotide metabolic process
|
GO_REF:0000004
|
IEA: Inferred from Electronic Annotation
|
SP_KW:KW-0546
|
P
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0004000
|
adenosine deaminase activity
|
GO_REF:0000002 GO_REF:0000003 GO_REF:0000020
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR006330 EC:3.5.4.4 HAMAP:MF_00540
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0019239
|
deaminase activity
|
GO_REF:0000002 GO_REF:0000002
|
IEA: Inferred from Electronic Annotation
|
InterPro:IPR001365 InterPro:IPR006650
|
F
|
Seeded from EcoCyc 12.5 <ref name = 'LIB:EcoCyc12.5'/>
|
complete
|-
|

|
GO:0005737
|
cytoplasm
|

|

|

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

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

|

|

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

|
GO:0005488
|
binding
|
PMID:3486673
|
ISS: Inferred from Sequence or Structural Similarity
|
UniProtKB:P56658
|
F
|
CHEBI:27834 (Deoxycoformycin mechanistically inhibits Add).
|
complete
|-
|

|
GO:0004000
|
adenosine deaminase activity
|
PMID:5335916
|
ISS: Inferred from Sequence or Structural Similarity
|
UniProtKB:P56658
|
F
|

|
complete
|-
|

|
GO:0004000
|
adenosine deaminase activity
|
PMID:4874315
|
IDA: Inferred from Direct Assay
|

|
F
|

|
complete

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.N46aa72e194b25&page=23273&pagename={{FULLPAGENAMEE}}&type=&template=GO_table_product edit table] || || || || || || || ||
|}


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

{{Product_interactions_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Partner Type!!Partner!!Notes!!References!!Evidence
|-
|
Protein
|
rpsM 
|

|
PMID:16606699
|
Experiment(s):EBI-1140315 
|-
|
Protein
|
arpA 
|

|
PMID:16606699
|
Experiment(s):EBI-1140315 
|-
|
Protein
|
rplT 
|

|
PMID:16606699
|
Experiment(s):EBI-1140315 
|-
|
Protein
|
insC1 
|

|
PMID:16606699
|
Experiment(s):EBI-1140315 
|-
|
Protein
|
ligA 
|

|
PMID:16606699
|
Experiment(s):EBI-1140315 
|-
|
Protein
|
gcd 
|

|
PMID:16606699
|
Experiment(s):EBI-1140315 
|-
|
Small Molecule
|
CHEBI:27834 (Deoxycoformycin)
|
Inhibitor of Add activity
|

|

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.H46aa72e958e91&page=23273&pagename={{FULLPAGENAMEE}}&type=&template=Product_interactions_table edit table] || || || ||
|}


</protect>
===Notes===

==Localization==

{{Product_localization_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Compartment!!Description!!Evidence!!Notes

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.L46a805074c1b0&page=23273&pagename={{FULLPAGENAMEE}}&type=&template=Product_localization_table edit table] || || ||
|}


<protect></protect>

===Notes===

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

{{Product_physical_properties_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Sequence
||
[http://biocyc.org/ECOLI/sequence-aa?object=ADENODEAMIN-MONOMER at EcoCyc]
<pre>MIDTTLPLTD IHRHLDGNIR PQTILELGRQ YNISLPAQSL ETLIPHVQVI ANEPDLVSFL
TKLDWGVKVL ASLDACRRVA FENIEDAARH GLHYVELRFS PGYMAMAHQL PVAGVVEAVI
DGVREGCRTF GVQAKLIGIM SRTFGEAACQ QELEAFLAHR DQITALDLAG DELGFPGSLF
LSHFNRARDA GWHITVHAGE AAGPESIWQA IRELGAERIG HGVKAIEDRA LMDFLAEQQI
GIESCLTSNI QTSTVAELAA HPLKTFLEHG IRASINTDDP GVQGVDIIHE YTVAAPAAGL
SREQIRQAQI NGLEMAFLSA EEKRALREKV AAK</pre>
|-
!align=left {{table heading style}} |Mol. Wt
||
36.4 kDa (calc) <ref name='LIB:EcoCyc10.6'/>
|-
!align=left {{table heading style}} |pI
||
5.63<ref name='LIB:EcoCyc10.6'/>
|-
!align=left {{table heading style}} |Extinction coefficient
||
22460 - 22960 (calc based on 4 Y, 3 W, and 4 C residues)

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.V46aa72eb37ca8&page=23273&pagename={{FULLPAGENAMEE}}&type=1&template=Product_phys_prop_table edit table] ||
|}


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

{{Product_domains_motifs_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table heading style}}
!|Type!!Residues!!Description!!Notes

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.M46aa72eb9d42b&page=23273&pagename={{FULLPAGENAMEE}}&type=&template=Product_motif_table edit table] || || ||
|}


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

{{Product_structure_help}}
{|border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"

|-
!align=left {{table heading style}} |Structures
||
<beststructure>add
562</beststructure>

|-
!align=left {{table heading style}} |Models
||

View models at:
* [http://dragon.bio.purdue.edu/ecolpredict2/localsearch/cgi-bin/search3.cgi?q=add&sub=keywordSearc EcoliPredict]
* [http://modbase.compbio.ucsf.edu/modbase-cgi/model_search.cgi?searchmode=default&displaymode=moddetail&searchproperties=ALL&searchvalue=add&organism=562&organismtext= ModBase]
* [http://bioinf.cs.ucl.ac.uk/psipred/ PSI-PRED]
* [http://www.ebi.ac.uk/msd-srv/pqs/ Protein Quaternary Structure] (PQS)
* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.H46a80508dcdd8&page=23273&pagename={{FULLPAGENAMEE}}&type=1&template=Product_structure_table edit table] ||
|}


</protect>
===Notes===

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

{{Product_resources_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Resource type!!Source!!Notes/Reference

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.U46aa72ec59068&page=23273&pagename={{FULLPAGENAMEE}}&type=&template=Product_resource_table edit table] || ||
|}


<protect></protect>
===Notes===

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

{{Gene_accessions_help}}
{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Database!!Accession!!Notes
|-
|
[http://ecocyc.org EcoCyc] ([[EcoCyc|EcoliWiki Page]])
|
[http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=ADENODEAMIN-MONOMER EcoCyc:ADENODEAMIN-MONOMER]
|

|-
|
[http://uniprot.org/ UniProt] ([[UniProt|EcoliWiki Page]])
|
[[uniprot:P22333|UniProt:P22333]]
|

|-
|
[http://pfam.sanger.ac.uk/ PFAM] ([[PFAM|EcoliWiki Page]])
|
[http://pfam.sanger.ac.uk/family?acc=PF00962 PFAM:PF00962]
|

|-
|
[http://www.ncbi.nlm.nih.gov/RefSeq/ RefSeq] ([[RefSeq|EcoliWiki Page]])
|
[http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide&val=NP_416140 RefSeq:NP_416140]
|

|-
|
[http://modbase.compbio.ucsf.edu ModBase] ([[ModBase|EcoliWiki Page]])
|
[http://salilab.org/modbase/searchbyid?databaseID=P22333 ModBase:P22333]
|

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.C46aa72ecb0698&page=23273&pagename={{FULLPAGENAMEE}}&type=0&template=Gene_accessions_table edit table] || ||
|}


<protect></protect>
===Notes===

==Links==
{{BacktoTop}}


{|class = 'sortable' border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;"
|- {{table_heading_style}}
!|Name!!URL!!Comments

|-class='sortbottom'
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=421aa90e079fa326b6494f812ad13e79.23273.F46a8050c4b2e7&page=23273&pagename={{FULLPAGENAMEE}}&type=0&template=Links_table edit table] || ||
|}


<noinclude>
==References==
{{BacktoTop}}

<references/>
__NOTOC__
</noinclude>
===Categories===
{{BacktoTop}}
[[Category:Proteins]]
[[Category:GO:0005737_!_cytoplasm]][[Category:GO:0015949_!_nucleobase, nucleoside and nucleotide interconversion]]