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ECOLI:6PGD

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) gnd
Protein Name(s) 6-phosphogluconate dehydrogenase, decarboxylating
External Links
UniProt P00350
EMBL K02072
M63821
M64326
M64327
M64328
M64329
M64330
M64331
U00096
AP009048
M23181
M18956
M18957
M18960
AF125322
PIR D64968
I62463
I62465
RefSeq NP_416533.1
YP_490272.1
PDB 2ZYA
2ZYD
3FWN
PDBsum 2ZYA
2ZYD
3FWN
ProteinModelPortal P00350
SMR P00350
DIP DIP-9819N
IntAct P00350
PRIDE P00350
EnsemblBacteria AAC75090
BAA15869
GeneID 12932360
946554
KEGG ecj:Y75_p1992
eco:b2029
PATRIC 32119393
EchoBASE EB0406
EcoGene EG10411
InParanoid P00350
KO K00033
OMA SDEYNWD
OrthoDB EOG6MSS4W
PhylomeDB P00350
BioCyc EcoCyc:6PGLUCONDEHYDROG-MONOMER
ECOL316407:JW2011-MONOMER
MetaCyc:6PGLUCONDEHYDROG-MONOMER
UniPathway UPA00115
EvolutionaryTrace P00350
PRO PR:P00350
Proteomes UP000000318
UP000000625
Genevestigator P00350
GO GO:0042802
GO:0050661
GO:0004616
GO:0042803
GO:0019521
GO:0006098
Gene3D 1.10.1040.10
1.20.5.320
3.40.50.720
InterPro IPR008927
IPR006114
IPR006113
IPR006115
IPR006184
IPR013328
IPR012284
IPR016040
Pfam PF00393
PF03446
PIRSF PIRSF000109
SUPFAM SSF48179
TIGRFAMs TIGR00873
PROSITE PS00461

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004616

phosphogluconate dehydrogenase (decarboxylating) activity

PMID:368027[1]

ECO:0000315

F

Table 3. A mutant that contains gnd on a plasmid has a significantly higher phosphogluconate dehydrogenase activity than the wild type.

complete

enables

GO:0042803

protein homodimerization activity

PMID:19686854[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P00350

F

Seeded From UniProt

complete

involved_in

GO:0006098

pentose-phosphate shunt

PMID:19686854[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004616

phosphogluconate dehydrogenase (decarboxylating) activity

PMID:19686854[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24561554[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P00350

F

Seeded From UniProt

complete

enables

GO:0004616

phosphogluconate dehydrogenase (decarboxylating) activity

PMID:4869212[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0046177

D-gluconate catabolic process

PMID:4869212[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004616

phosphogluconate dehydrogenase (decarboxylating) activity

PMID:4387807[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004616

phosphogluconate dehydrogenase (decarboxylating) activity

PMID:35519[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004616

phosphogluconate dehydrogenase (decarboxylating) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006113
InterPro:IPR006114
InterPro:IPR006183
InterPro:IPR006184

F

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:IPR006113
InterPro:IPR006114
InterPro:IPR006184

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013328

F

Seeded From UniProt

complete

enables

GO:0050661

NADP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006115

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:IPR006113
InterPro:IPR006114
InterPro:IPR006183
InterPro:IPR006184
InterPro:IPR008927
InterPro:IPR013328

P

Seeded From UniProt

complete

enables

GO:0004616

phosphogluconate dehydrogenase (decarboxylating) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.1.1.44

F

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

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: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:0019521

D-gluconate metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0311

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 2.2 Chen, YY et al. (2010) Conformational changes associated with cofactor/substrate binding of 6-phosphogluconate dehydrogenase from Escherichia coli and Klebsiella pneumoniae: Implications for enzyme mechanism. J. Struct. Biol. 169 25-35 PubMed GONUTS page
  3. ↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
  4. ↑ 4.0 4.1 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
  5. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  6. ↑ 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
  7. ↑ Sly, LI & Doelle, HW (1968) 6-phosphogluconate dehydrogenase in cell free extracts of Escherichia coli K-12. Arch Mikrobiol 63 214-23 PubMed GONUTS page
  8. ↑ Wolf, RE Jr & Shea, FM (1979) Combined use of strain construction and affinity chromatography in the rapid, high-yield purification of 6-phosphogluconate dehydrogenase from Escherichia coli. J. Bacteriol. 138 171-5 PubMed GONUTS page
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