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ECOLI:KBAY

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) kbaY (synonyms: agaY, kba, yraC)
Protein Name(s) D-tagatose-1,6-bisphosphate aldolase subunit KbaY

TBPA TagBP aldolase D-tagatose-bisphosphate aldolase class II Ketose 1,6-bisphosphate aldolase class II Tagatose-bisphosphate aldolase

External Links
UniProt P0AB74
EMBL U18997
U00096
AP009048
PIR E65103
RefSeq NP_417606.1
YP_491324.1
PDB 1GVF
PDBsum 1GVF
ProteinModelPortal P0AB74
SMR P0AB74
DIP DIP-47961N
IntAct P0AB74
MINT MINT-1279079
STRING 511145.b3137
PRIDE P0AB74
EnsemblBacteria AAC76171
BAE77183
GeneID 12932161
947644
KEGG ecj:Y75_p3059
eco:b3137
PATRIC 32121692
EchoBASE EB2621
EcoGene EG12768
HOGENOM HOG000227793
InParanoid P0AB74
KO K08302
OMA GENFLRH
OrthoDB EOG6HXJ7B
PhylomeDB P0AB74
BioCyc EcoCyc:TAGAALDOL1-MONOMER
ECOL316407:JW3106-MONOMER
MetaCyc:TAGAALDOL1-MONOMER
SABIO-RK P0AB74
UniPathway UPA00704
EvolutionaryTrace P0AB74
PRO PR:P0AB74
Proteomes UP000000318
UP000000625
Genevestigator P0AB74
GO GO:0009025
GO:0008270
GO:0005975
GO:2001059
Gene3D 3.20.20.70
HAMAP MF_01293
InterPro IPR013785
IPR000771
IPR023788
IPR011288
Pfam PF01116
PIRSF PIRSF001359
TIGRFAMs TIGR00167
TIGR01858
PROSITE PS00602
PS00806

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0009025

tagatose-bisphosphate aldolase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12419
EcoGene:EG12768
PANTHER:PTN002410818

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12768
PANTHER:PTN002410818

C

Seeded From UniProt

complete

enables

GO:0009025

tagatose-bisphosphate aldolase activity

PMID:11976750[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0051289

protein homotetramerization

PMID:10712619[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:10712619[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0009025

tagatose-bisphosphate aldolase activity

PMID:10712619[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:11940603[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013785

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000771
InterPro:IPR011288
InterPro:IPR023788

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000771
InterPro:IPR011288
InterPro:IPR023788

F

Seeded From UniProt

complete

enables

GO:0009025

tagatose-bisphosphate aldolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011288
InterPro:IPR023788

F

Seeded From UniProt

complete

enables

GO:0016832

aldehyde-lyase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000771

F

Seeded From UniProt

complete

involved_in

GO:2001059

D-tagatose 6-phosphate catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR023788

P

Seeded From UniProt

complete

enables

GO:0009025

tagatose-bisphosphate aldolase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.1.2.40

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101702

F

Seeded From UniProt

complete

enables

GO:0009025

tagatose-bisphosphate aldolase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101702

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101702

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

involved_in

GO:2001059

D-tagatose 6-phosphate catabolic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00704

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. Brinkkötter, A et al. (2002) Two class II D-tagatose-bisphosphate aldolases from enteric bacteria. Arch. Microbiol. 177 410-9 PubMed GONUTS page
  3. 3.0 3.1 3.2 Zgiby, SM et al. (2000) Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases. Eur. J. Biochem. 267 1858-68 PubMed GONUTS page
  4. Hall, DR et al. (2002) Structure of tagatose-1,6-bisphosphate aldolase. Insight into chiral discrimination, mechanism, and specificity of class II aldolases. J. Biol. Chem. 277 22018-24 PubMed GONUTS page
  5. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page