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BACSU:TAL

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Species (Taxon ID) Bacillus subtilis (strain 168). (224308)
Gene Name(s) tal (synonyms: ywjH)
Protein Name(s) Transaldolase

20 kDa phosphoprotein OrfU CSI9

External Links
UniProt P19669
EMBL M22039
Z49782
AL009126
PIR F32354
RefSeq NP_391592.3
PDB 3R8R
PDBsum 3R8R
ProteinModelPortal P19669
SMR P19669
IntAct P19669
MINT MINT-8300511
STRING 224308.BSU37110
PhosSite P0802267
PaxDb P19669
EnsemblBacteria CAB15728
GeneID 938462
KEGG bsu:BSU37110
PATRIC 18979458
GenoList BSU37110
eggNOG COG0176
HOGENOM HOG000226073
InParanoid P19669
KO K00616
OMA KDWEKVP
OrthoDB EOG6PS600
PhylomeDB P19669
BioCyc BSUB:BSU37110-MONOMER
UniPathway UPA00115
Proteomes UP000001570
GO GO:0005737
GO:0042802
GO:0004801
GO:0006098
Gene3D 3.20.20.70
HAMAP MF_00494
InterPro IPR013785
IPR001585
IPR004731
IPR022999
IPR018225
PANTHER PTHR10683
Pfam PF00923
TIGRFAMs TIGR00875
PROSITE PS01054
PS00958

Annotations

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

enables

GO:0097023

fructose 6-phosphate aldolase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11905
EcoGene:EG13471
PANTHER:PTN000074413

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:22212631[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P19669

F

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:IPR022999

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:IPR001585
InterPro:IPR004731
InterPro:IPR018225

P

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:IPR033919

F

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:UR000103165

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:UR000103165

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:UR000103165

F

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

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

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

Notes

References

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

  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. Samland, AK et al. (2012) Conservation of structure and mechanism within the transaldolase enzyme family. FEBS J. 279 766-78 PubMed GONUTS page