fbaA:Gene Product(s): Difference between revisions

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!align=left {{table heading style}} |Standard name
!align=left |Standard name
||
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FbaA  
FbaA  
|-
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!align=left {{table heading style}} |Synonyms
!align=left |Synonyms
||
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fructose-bisphosphate aldolase, class II<ref name='LIB:Riley_2006'/>, B2925<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Fda<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Ald<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, FbaA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Fba<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>  
fructose-bisphosphate aldolase, class II<ref name='LIB:Riley_2006'/>, B2925<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Fda<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Ald<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, FbaA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Fba<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>  
|-
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!align=left {{table heading style}} |Product description
!align=left |Product description
||
||
fructose bisphosphate aldolase<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;  
fructose bisphosphate aldolase<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;  
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Fructose-bisphosphate aldolase, class II; binds Zn(II); homdomeric<ref name='LIB:EcoGene'/>
Fructose-bisphosphate aldolase, class II; binds Zn(II); homdomeric<ref name='LIB:EcoGene'/>
|-
|-
!align=left {{table heading style}} |EC number (for enzymes)
!align=left |EC number (for enzymes)
||
||
* [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13]<ref name='LIB:Riley_2006'/>
* [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13]<ref name='LIB:Riley_2006'/>


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!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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complete  
complete  


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!|Partner Type!!Partner!!Notes!!References!!Evidence
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Experiment(s):EBI-879773<br />  
Experiment(s):EBI-879773<br />  


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!|Compartment!!Description!!Evidence!!Source!!Notes
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PMID:2649077
PMID:2649077
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[http://www.york.ac.uk/res/thomas/Echolocation.cfm?EB_SubLocID=EB0278 EchoLocation:fbaA]
[http://www.york.ac.uk/res/thomas/Echolocation.cfm?EB_SubLocID=EB0278 EchoLocation:fbaA]
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|-
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!align=left {{table heading style}} |Sequence
!align=left |Sequence
||
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[http://biocyc.org/ECOLI/sequence-aa?object=FRUCTBISALD-CLASSII-MONOMER at EcoCyc]  
[http://biocyc.org/ECOLI/sequence-aa?object=FRUCTBISALD-CLASSII-MONOMER at EcoCyc]  
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LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF QELNAIDVL</pre>  
LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF QELNAIDVL</pre>  
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!align=left {{table heading style}} |Length
!align=left |Length
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359
359
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!align=left {{table heading style}} |Mol. Wt
!align=left |Mol. Wt
||
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39.146 kDa
39.146 kDa
|-
|-
!align=left {{table heading style}} |pI
!align=left |pI
||
||
5.8 (calculated)
5.8 (calculated)
|-
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!align=left {{table heading style}} |Extinction coefficient
!align=left |Extinction coefficient
||
||
41,370 - 41,870 (calc based on 13 Y, 4 W, and 4 C residues)
41,370 - 41,870 (calc based on 13 Y, 4 W, and 4 C residues)


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[http://www.uniprot.org/uniprot/P0AB71#section_features UniProt:P0AB71]  
[http://www.uniprot.org/uniprot/P0AB71#section_features UniProt:P0AB71]  


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<beststructure>
<beststructure>
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</beststructure>
</beststructure>
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!align=left {{table heading style}} |Models
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View models at:
View models at:
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* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)
* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)


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Revision as of 01:01, 9 January 2010

{{#css:Suppresslinks.css}}<css>h1 .editsection { display:none;} h2 .editsection { display:none;}</css>

Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

FbaA

Synonyms

fructose-bisphosphate aldolase, class II[1], B2925[2][1], Fda[2][1], Ald[2][1], FbaA[2][1], Fba[2][1]

Product description

fructose bisphosphate aldolase[2][3];

Component of fructose bisphosphate aldolase class II[2][3]

Fructose-bisphosphate aldolase, class II; binds Zn(II); homdomeric[4]

EC number (for enzymes)
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Notes

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference(s) Evidence Code with/from Aspect Notes Status
GO:0046872

metal ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc [5]

complete

GO:0016829

lyase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0456

F

Seeded from EcoCyc [5]

complete

GO:0008270

zinc ion binding

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR000771
SP_KW:KW-0862

F

Seeded from EcoCyc [5]

complete

GO:0008152

metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013785

P

Seeded from EcoCyc [5]

complete

GO:0006096

glycolysis

GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR000771
InterPro:IPR006411
SP_KW:KW-0324

P

Seeded from EcoCyc [5]

complete

GO:0004332

fructose-bisphosphate aldolase activity

GO_REF:0000002
GO_REF:0000002
GO_REF:0000003

IEA: Inferred from Electronic Annotation

InterPro:IPR000771
InterPro:IPR006411
EC:4.1.2.13

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0003824

catalytic activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013785

F

Seeded from EcoCyc [5]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P0A6Y8

F

Seeded from EcoCyc [5]

complete

GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

required fields missing

GO:0016052

carbohydrate catabolic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0004332

fructose-bisphosphate aldolase activity

PMID:16562136[8]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0006094

gluconeogenesis

P

required field missing

GO:0004332

fructose-bisphosphate aldolase activity

PMID:16562136[8]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0008270

zinc ion binding

PMID:11985624[9]

IDA: Inferred from Direct Assay

F

complete

GO:0004332

fructose-bisphosphate aldolase activity

PMID:16562136[8]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0008270

zinc ion binding

PMID:8436219[10]

IDA: Inferred from Direct Assay

F

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of fructose bisphosphate aldolase class II

could be indirect

Protein

dnaK

PMID:15690043[7]

Experiment(s):EBI-879773, EBI-884401

Protein

fldA

PMID:15690043[7]

Experiment(s):EBI-879773

Protein

hsdR

PMID:15690043[7]

Experiment(s):EBI-879773

Protein

rpsB

PMID:15690043[7]

Experiment(s):EBI-879773

Protein

yfeR

PMID:15690043[7]

Experiment(s):EBI-879773
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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Source Notes

Cytoplasm

PMID:2649077[11]

EchoLocation:fbaA


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Notes

Structure and Physical Properties

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Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Sequence

at EcoCyc 

MSKIFDFVKP GVITGDDVQK VFQVAKENNF ALPAVNCVGT DSINAVLETA AKVKAPVIVQ
FSNGGASFIA GKGVKSDVPQ GAAILGAISG AHHVHQMAEH YGVPVILHTD HCAKKLLPWI
DGLLDAGEKH FAATGKPLFS SHMIDLSEES LQENIEICSK YLERMSKIGM TLEIELGCTG
GEEDGVDNSH MDASALYTQP EDVDYAYTEL SKISPRFTIA ASFGNVHGVY KPGNVVLTPT
ILRDSQEYVS KKHNLPHNSL NFVFHGGSGS TAQEIKDSVS YGVVKMNIDT DTQWATWEGV
LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF QELNAIDVL
Length

359

Mol. Wt

39.146 kDa

pI

5.8 (calculated)

Extinction coefficient

41,370 - 41,870 (calc based on 13 Y, 4 W, and 4 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes

Initiator Methionine

1

Removed

UniProt:P0AB71

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<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=fbaA taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:FRUCTBISALD-CLASSII-MONOMER

UniProt (EcoliWiki Page)

UniProt:P0AB71

PFAM (EcoliWiki Page)

PFAM:PF01116

RefSeq (EcoliWiki Page)

RefSeq:NP_417400


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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  6. ↑ EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  7. ↑ 7.0 7.1 7.2 7.3 7.4 7.5 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  8. ↑ 8.0 8.1 8.2 Böck, A & Neidhardt, FC (1966) Isolation of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase Activity. J. Bacteriol. 92 464-9 PubMed
  9. ↑ Katayama, A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur. J. Biochem. 269 2403-13 PubMed
  10. ↑ Berry, A & Marshall, KE (1993) Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli. FEBS Lett. 318 11-6 PubMed
  11. ↑ Alefounder, PR et al. (1989) Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli. Biochem. J. 257 529-34 PubMed

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