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ECOLI:G6PI

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) pgi
Protein Name(s) Glucose-6-phosphate isomerase

GPI Phosphoglucose isomerase PGI Phosphohexose isomerase PHI

External Links
UniProt P0A6T1
EMBL X15196
U00006
U00096
AP009048
PIR H65209
RefSeq NP_418449.1
YP_492168.1
PDB 3NBU
PDBsum 3NBU
ProteinModelPortal P0A6T1
SMR P0A6T1
DIP DIP-35887N
IntAct P0A6T1
STRING 511145.b4025
PhosSite P0810418
PaxDb P0A6T1
PRIDE P0A6T1
EnsemblBacteria AAC76995
BAE78027
GeneID 12932965
948535
KEGG ecj:Y75_p3912
eco:b4025
PATRIC 32123579
EchoBASE EB0696
EcoGene EG10702
eggNOG COG0166
HOGENOM HOG000261371
InParanoid P0A6T1
KO K01810
OMA FELANDC
OrthoDB EOG64R61J
PhylomeDB P0A6T1
BioCyc EcoCyc:PGLUCISOM
ECOL316407:JW3985-MONOMER
MetaCyc:PGLUCISOM
SABIO-RK P0A6T1
UniPathway UPA00109
EvolutionaryTrace P0A6T1
PRO PR:P0A6T1
Proteomes UP000000318
UP000000625
Genevestigator P0A6T1
GO GO:0005829
GO:0004347
GO:0042802
GO:0034599
GO:0006094
GO:0006096
Gene3D 1.10.1390.10
HAMAP MF_00473
InterPro IPR001672
IPR023096
IPR018189
PANTHER PTHR11469
Pfam PF00342
PRINTS PR00662
PROSITE PS00765
PS00174
PS51463

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004347

glucose-6-phosphate isomerase activity

PMID:368027[1]

ECO:0000315

F

Table 3. A much higher than normal level of Phosphoglucose isomerase activity is conferred when a plasmid carrying pgi is introduced to the strain.

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:0051156

glucose 6-phosphate metabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000157839
RGD:2727

P

Seeded From UniProt

complete

enables

GO:0048029

monosaccharide binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000157839
RGD:2727

F

Seeded From UniProt

complete

enables

GO:0016866

intramolecular transferase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000157839
RGD:2727

F

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:EG10702
MGI:MGI:95797
PANTHER:PTN000157839
SGD:S000000400
UniProtKB:P9WN69

P

Seeded From UniProt

complete

involved_in

GO:0006094

gluconeogenesis

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000157839
SGD:S000000400

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:EG10702
FB:FBgn0003074
PANTHER:PTN000157839
RGD:2727
TAIR:locus:2121929
TAIR:locus:2165462
UniProtKB:P06744

C

Seeded From UniProt

complete

enables

GO:0004347

glucose-6-phosphate isomerase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10702
FB:FBgn0003074
MGI:MGI:95797
PANTHER:PTN000157839
RGD:2727
SGD:S000000400
UniProtKB:P9WN69
UniProtKB:Q59000

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24561554[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6T1

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6T1

F

Seeded From UniProt

complete

involved_in

GO:0034599

cellular response to oxidative stress

PMID:18368388[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034599

cellular response to oxidative stress

PMID:18368388[5]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:5337843[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004347

glucose-6-phosphate isomerase activity

PMID:5328748[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004347

glucose-6-phosphate isomerase activity

PMID:7004378[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004347

glucose-6-phosphate isomerase activity

PMID:17239859[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004347

glucose-6-phosphate isomerase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001672
InterPro:IPR018189
InterPro:IPR023096

F

Seeded From UniProt

complete

involved_in

GO:0006094

gluconeogenesis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001672
InterPro:IPR018189

P

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:IPR001672
InterPro:IPR018189
InterPro:IPR023096

P

Seeded From UniProt

complete

enables

GO:0004347

glucose-6-phosphate isomerase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:5.3.1.9

F

Seeded From UniProt

complete

involved_in

GO:0006094

gluconeogenesis

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000102780

P

Seeded From UniProt

complete

enables

GO:0004347

glucose-6-phosphate isomerase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000102780

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:UR000102780

C

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:UR000102780

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

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

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0312

P

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 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 3.6 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. ↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
  5. ↑ 5.0 5.1 Rungrassamee, W et al. (2008) Activation of glucose transport under oxidative stress in Escherichia coli. Arch. Microbiol. 190 41-9 PubMed GONUTS page
  6. ↑ Fraenkel, DG & Levisohn, SR (1967) Glucose and gluconate metabolism in an Escherichia coli mutant lacking phosphoglucose isomerase. J. Bacteriol. 93 1571-8 PubMed GONUTS page
  7. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  8. ↑ Loomis, WF Jr & Magasanik, B (1966) Nature of the effector of catabolite repression of beta-galactosidase in Escherichia coli. J. Bacteriol. 92 170-7 PubMed GONUTS page
  9. ↑ Schreyer, R & Böck, A (1980) Phosphoglucose isomerase from Escherischia coli K 10: purification, properties and formation under aerobic and anaerobic condition. Arch. Microbiol. 127 289-98 PubMed GONUTS page
  10. ↑ Ishii, N et al. (2007) Dynamic simulation of an in vitro multi-enzyme system. FEBS Lett. 581 413-20 PubMed GONUTS page
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