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ECOLI:TPIS

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) tpiA (ECO:0000255 with HAMAP-Rule:MF_00147) (synonyms: tpi)
Protein Name(s) Triosephosphate isomerase (ECO:0000255 with HAMAP-Rule:MF_00147)

TIM (ECO:0000255 with HAMAP-Rule:MF_00147) Triose-phosphate isomerase (ECO:0000255 with HAMAP-Rule:MF_00147)

External Links
UniProt P0A858
EMBL X00617
L19201
U00096
AP009048
PIR B65198
RefSeq NP_418354.1
YP_491532.1
PDB 1TMH
1TRE
PDBsum 1TMH
1TRE
ProteinModelPortal P0A858
SMR P0A858
DIP DIP-31849N
IntAct P0A858
MINT MINT-1228759
STRING 511145.b3919
SWISS-2DPAGE P0A858
PaxDb P0A858
PRIDE P0A858
EnsemblBacteria AAC76901
BAE77391
GeneID 12933653
948409
KEGG ecj:Y75_p3268
eco:b3919
PATRIC 32123351
EchoBASE EB1008
EcoGene EG11015
eggNOG COG0149
HOGENOM HOG000226413
InParanoid P0A858
KO K01803
OMA EANRICG
OrthoDB EOG66QM23
PhylomeDB P0A858
BioCyc EcoCyc:TPI-MONOMER
ECOL316407:JW3890-MONOMER
MetaCyc:TPI-MONOMER
SABIO-RK P0A858
UniPathway UPA00109
UPA00138
EvolutionaryTrace P0A858
PRO PR:P0A858
Proteomes UP000000318
UP000000625
Genevestigator P0A858
GO GO:0005829
GO:0016020
GO:0042802
GO:0004807
GO:0006094
GO:0006096
GO:0006098
Gene3D 3.20.20.70
HAMAP MF_00147_B
InterPro IPR013785
IPR022896
IPR000652
IPR020861
PANTHER PTHR21139
Pfam PF00121
SUPFAM SSF51351
TIGRFAMs TIGR00419
PROSITE PS00171
PS51440

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004807

triose-phosphate isomerase activity

PMID:368027[1]

ECO:0000316

UniProtKB:P0A796


F

Table 2. A mutant strain that has pfkA and tpi deleted has no triose-phophate isomerase activity. This is confirmed by another mutant that had only pfkA deleted and that had a normal level of triose-phosohate isomerase.

complete

part_of

GO:0016020

membrane

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0046166

glyceraldehyde-3-phosphate biosynthetic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000474559
UniProtKB:Q9SKP6

P

Seeded From UniProt

complete

involved_in

GO:0019563

glycerol catabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000474559
UniProtKB:Q9SKP6

P

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11015
FB:FBgn0086355
PANTHER:PTN000474559
SGD:S000002457
UniProtKB:P9WG43

P

Seeded From UniProt

complete

involved_in

GO:0006094

gluconeogenesis

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11015
PANTHER:PTN000474559
UniProtKB:P9WG43

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:EG11015
PANTHER:PTN000474559
RGD:3896
UniProtKB:P9WG43
UniProtKB:Q9SKP6

C

Seeded From UniProt

complete

enables

GO:0004807

triose-phosphate isomerase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11015
FB:FBgn0086355
MGI:MGI:98797
PANTHER:PTN000474559
PomBase:SPCC24B10.21
RGD:3896
SGD:S000002457
UniProtKB:P60174
UniProtKB:P9WG43
UniProtKB:Q7KQM0
UniProtKB:Q9SKP6

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24627523[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A858

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A858

F

Seeded From UniProt

complete

involved_in

GO:0006094

gluconeogenesis

PMID:11947134[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004807

triose-phosphate isomerase activity

PMID:6214548[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004807

triose-phosphate isomerase activity

PMID:6092857[7]

ECO:0000247

sequence alignment evidence used in manual assertion

UniProtKB:P00943

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:11947134[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004807

triose-phosphate isomerase activity

PMID:8309937[10]

ECO:0000314

direct assay evidence used in manual assertion

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:0004807

triose-phosphate isomerase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000652
InterPro:IPR020861
InterPro:IPR022896
InterPro:IPR035990

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR022896

P

Seeded From UniProt

complete

enables

GO:0004807

triose-phosphate isomerase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:5.3.1.1

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:UR000079063

C

Seeded From UniProt

complete

involved_in

GO:0006094

gluconeogenesis

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079063

P

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079063

P

Seeded From UniProt

complete

enables

GO:0004807

triose-phosphate isomerase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079063

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

involved_in

GO:0006094

gluconeogenesis

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0312
UniPathway:UPA00138

P

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0324
UniPathway:UPA00109

P

Seeded From UniProt

complete

enables

GO:0016853

isomerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0413

F

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ Thomson, J et al. (1979) ColE1 hybrid plasmids for Escherichia coli genes of glycolysis and the hexose monophosphate shunt. J. Bacteriol. 137 502-6 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 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
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 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. ↑ Häuser, R et al. (2014) A second-generation protein-protein interaction network of Helicobacter pylori. Mol. Cell Proteomics 13 1318-29 PubMed GONUTS page
  5. ↑ 5.0 5.1 Anderson, A & Cooper, RA (1969) Gluconeogenesis in Escherichia coli The role of triose phosphate isomerase. FEBS Lett. 4 19-20 PubMed GONUTS page
  6. ↑ Shimosaka, M et al. (1982) Application of hybrid plasmids carrying glycolysis genes to ATP production by Escherichia coli. J. Bacteriol. 152 98-103 PubMed GONUTS page
  7. ↑ Pichersky, E et al. (1984) Nucleotide sequence of the triose phosphate isomerase gene of Escherichia coli. Mol. Gen. Genet. 195 314-20 PubMed GONUTS page
  8. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  9. ↑ 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
  10. ↑ Mainfroid, V et al. (1993) Replacing the (beta alpha)-unit 8 of E.coli TIM with its chicken homologue leads to a stable and active hybrid enzyme. Protein Eng. 6 893-900 PubMed GONUTS page
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