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ECOLI:G6PD

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) zwf (ECO:0000255 with HAMAP-Rule:MF_00966)
Protein Name(s) Glucose-6-phosphate 1-dehydrogenase (ECO:0000255 with HAMAP-Rule:MF_00966)

G6PD (ECO:0000255 with HAMAP-Rule:MF_00966) Extracellular death factor EDF

External Links
UniProt P0AC53
EMBL M55005
U00096
AP009048
U13783
U13784
U13785
U13786
U13787
U13788
U13789
U13790
U13791
U13792
U13793
U13794
X63694
PIR D64947
RefSeq NP_416366.1
YP_490114.1
ProteinModelPortal P0AC53
SMR P0AC53
DIP DIP-35780N
IntAct P0AC53
MINT MINT-1317139
STRING 511145.b1852
SWISS-2DPAGE P0AC53
PaxDb P0AC53
PRIDE P0AC53
EnsemblBacteria AAC74922
BAA15660
GeneID 12930160
946370
KEGG ecj:Y75_p1828
eco:b1852
PATRIC 32119025
EchoBASE EB1203
EcoGene EG11221
eggNOG COG0364
HOGENOM HOG000046191
InParanoid P0AC53
KO K00036
OMA HNLQTTK
OrthoDB EOG61308Z
PhylomeDB P0AC53
BioCyc EcoCyc:GLU6PDEHYDROG-MONOMER
ECOL316407:JW1841-MONOMER
MetaCyc:GLU6PDEHYDROG-MONOMER
UniPathway UPA00115
PRO PR:P0AC53
Proteomes UP000000318
UP000000625
Genevestigator P0AC53
GO GO:0004345
GO:0042802
GO:0050661
GO:0006006
GO:0006098
GO:0009372
Gene3D 3.40.50.720
HAMAP MF_00966
InterPro IPR001282
IPR019796
IPR022675
IPR022674
IPR016040
PANTHER PTHR23429
Pfam PF02781
PF00479
PIRSF PIRSF000110
PRINTS PR00079
TIGRFAMs TIGR00871
PROSITE PS00069

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004345

glucose-6-phosphate dehydrogenase activity

PMID:368027[1]

ECO:0000315

F

Table 3. A mutant strain that does not contain zwf has a significantly lower level of glucose-6-phosphate dehydrogenase activity than the wild type.

complete

enables

GO:0042802

identical protein binding

PMID:19698713[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AC53

F

Seeded From UniProt

complete

enables

GO:0004345

glucose-6-phosphate dehydrogenase activity

PMID:4869212[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0010699

cell-cell signaling involved in quorum sensing

PMID:18310334[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006098

pentose-phosphate shunt

PMID:14645264[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006006

glucose metabolic process

PMID:14645264[5]

ECO:0000315

mutant phenotype 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

enables

GO:0004345

glucose-6-phosphate dehydrogenase activity

PMID:4401601[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004345

glucose-6-phosphate dehydrogenase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR019796
InterPro:IPR022674
InterPro:IPR022675

F

Seeded From UniProt

complete

involved_in

GO:0006006

glucose metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001282
InterPro:IPR019796
InterPro:IPR022674
InterPro:IPR022675

P

Seeded From UniProt

complete

enables

GO:0050661

NADP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR022674
InterPro:IPR022675

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001282
InterPro:IPR019796
InterPro:IPR022674
InterPro:IPR022675

P

Seeded From UniProt

complete

enables

GO:0004345

glucose-6-phosphate dehydrogenase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.1.1.49

F

Seeded From UniProt

complete

enables

GO:0004345

glucose-6-phosphate dehydrogenase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000184474

F

Seeded From UniProt

complete

enables

GO:0050661

NADP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000184474

F

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:UR000184474

P

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0119

P

Seeded From UniProt

complete

involved_in

GO:0006006

glucose metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0313

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0009372

quorum sensing

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0673

P

Seeded From UniProt

complete

involved_in

GO:0006098

pentose-phosphate shunt

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00115

P

Seeded From UniProt

complete

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. Acebrón, SP et al. (2009) DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface. FEBS Lett. 583 2991-6 PubMed GONUTS page
  3. Fraenkel, DG (1968) Selection of Escherichia coli mutants lacking glucose-6-phosphate dehydrogenase or gluconate-6-phosphate dehydrogenase. J. Bacteriol. 95 1267-71 PubMed GONUTS page
  4. Kolodkin-Gal, I & Engelberg-Kulka, H (2008) The extracellular death factor: physiological and genetic factors influencing its production and response in Escherichia coli. J. Bacteriol. 190 3169-75 PubMed GONUTS page
  5. 5.0 5.1 Hua, Q et al. (2003) Responses of the central metabolism in Escherichia coli to phosphoglucose isomerase and glucose-6-phosphate dehydrogenase knockouts. J. Bacteriol. 185 7053-67 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. Banerjee, S & Fraenkel, DG (1972) Glucose-6-phosphate dehydrogenase from Escherichia coli and from a "high-level" mutant. J. Bacteriol. 110 155-60 PubMed GONUTS page