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ECOLI:TALB

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) talB (synonyms: yaaK)
Protein Name(s) Transaldolase B
External Links
UniProt P0A870
EMBL D13161
S80045
U00096
AP009048
PIR S40535
RefSeq NP_414549.1
YP_488314.1
PDB 1I2N
1I2O
1I2P
1I2Q
1I2R
1ONR
1UCW
3KOF
PDBsum 1I2N
1I2O
1I2P
1I2Q
1I2R
1ONR
1UCW
3KOF
ProteinModelPortal P0A870
SMR P0A870
DIP DIP-31850N
IntAct P0A870
STRING 511145.b0008
PhosSite P0810439
SWISS-2DPAGE P0A870
PaxDb P0A870
PRIDE P0A870
EnsemblBacteria AAC73119
BAB96586
GeneID 12932945
944748
KEGG ecj:Y75_p0008
eco:b0008
PATRIC 32115111
EchoBASE EB1517
EcoGene EG11556
eggNOG COG0176
HOGENOM HOG000281234
InParanoid P0A870
KO K00616
OMA FNAIDEY
OrthoDB EOG6G7R4D
PhylomeDB P0A870
BioCyc ECOL316407:JW0007-MONOMER
UniPathway UPA00115
EvolutionaryTrace P0A870
PRO PR:P0A870
Proteomes UP000000318
UP000000625
Genevestigator P0A870
GO GO:0005829
GO:0016020
GO:0004801
GO:0006098
Gene3D 3.20.20.70
HAMAP MF_00492
InterPro IPR013785
IPR001585
IPR004730
IPR018225
PANTHER PTHR10683
Pfam PF00923
TIGRFAMs TIGR00874
PROSITE PS01054
PS00958

Annotations

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

part_of

GO:0016020

membrane

PMID:16858726[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004801

sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity

PMID:7592346[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009052

pentose-phosphate shunt, non-oxidative branch

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11556
PANTHER:PTN002581147
RGD:620674

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11556
EcoGene:EG11797
PANTHER:PTN001321958

C

Seeded From UniProt

complete

enables

GO:0004801

sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11556
PANTHER:PTN002581146
RGD:620674
SGD:S000003275
SGD:S000004346
UniProtKB:P37837
UniProtKB:Q5BGU0

F

Seeded From UniProt

complete

enables

GO:0016744

transferase activity, transferring aldehyde or ketonic groups

PMID:9883893[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009052

pentose-phosphate shunt, non-oxidative branch

PMID:11298760[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[7]

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

enables

GO:0004801

sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004730

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004730

C

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:IPR001585
InterPro:IPR018225

P

Seeded From UniProt

complete

involved_in

GO:0006098

pentose-phosphate shunt

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004730

P

Seeded From UniProt

complete

enables

GO:0004801

sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.2.1.2

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000103161

C

Seeded From UniProt

complete

involved_in

GO:0006098

pentose-phosphate shunt

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000103161

P

Seeded From UniProt

complete

enables

GO:0004801

sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000103161

F

Seeded From UniProt

complete

involved_in

GO:0006098

pentose-phosphate shunt

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0570
UniPathway:UPA00115

P

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

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Notes

References

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

  1. ↑ 1.0 1.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  2. ↑ Sprenger, GA et al. (1995) Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains. J. Bacteriol. 177 5930-6 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ Schörken, U et al. (1998) Disruption of Escherichia coli transaldolase into catalytically active monomers: evidence against half-of-the-sites mechanism. FEBS Lett. 441 247-50 PubMed GONUTS page
  5. ↑ Schörken, U et al. (2001) Identification of catalytically important residues in the active site of Escherichia coli transaldolase. Eur. J. Biochem. 268 2408-15 PubMed GONUTS page
  6. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  7. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
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