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ECOLI:DHG

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) gcd
Protein Name(s) Quinoprotein glucose dehydrogenase

Glucose dehydrogenase [pyrroloquinoline-quinone]

External Links
UniProt P15877
EMBL X51323
D12651
U00096
AP009048
PIR D64735
RefSeq NP_414666.1
YP_488427.1
ProteinModelPortal P15877
SMR P15877
DIP DIP-9747N
IntAct P15877
MINT MINT-1267882
STRING 511145.b0124
PaxDb P15877
PRIDE P15877
EnsemblBacteria AAC73235
BAB96699
GeneID 12932964
944830
KEGG ecj:Y75_p0121
eco:b0124
PATRIC 32115351
EchoBASE EB0364
EcoGene EG10369
eggNOG COG4993
HOGENOM HOG000116843
InParanoid P15877
KO K00117
OMA DGDWPAY
OrthoDB EOG68Q0MR
PhylomeDB P15877
BioCyc EcoCyc:GLUCDEHYDROG-MONOMER
ECOL316407:JW0120-MONOMER
MetaCyc:GLUCDEHYDROG-MONOMER
RETL1328306-WGS:GSTH-1225-MONOMER
BRENDA 1.1.5.2
PRO PR:P15877
Proteomes UP000000318
UP000000625
Genevestigator P15877
GO GO:0016021
GO:0030288
GO:0005886
GO:0000287
GO:0070968
GO:0008876
GO:0048039
GO:0019595
Gene3D 2.140.10.10
InterPro IPR017511
IPR018391
IPR002372
IPR027295
IPR011047
IPR001479
Pfam PF01011
SMART SM00564
SUPFAM SSF50998
TIGRFAMs TIGR03074
PROSITE PS00363
PS00364

Annotations

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

enables

GO:0008876

quinoprotein glucose dehydrogenase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10369
PANTHER:PTN000793792

F

Seeded From UniProt

complete

enables

GO:0070968

pyrroloquinoline quinone binding

PMID:9705344[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0048039

ubiquinone binding

PMID:14612441[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

PMID:8509415[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008876

quinoprotein glucose dehydrogenase activity

PMID:8509415[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:12686133[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017511

C

Seeded From UniProt

complete

enables

GO:0016614

oxidoreductase activity, acting on CH-OH group of donors

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017511

F

Seeded From UniProt

complete

part_of

GO:0030288

outer membrane-bounded periplasmic space

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001479

C

Seeded From UniProt

complete

enables

GO:0048038

quinone binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017511

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:IPR001479
InterPro:IPR017511

P

Seeded From UniProt

complete

enables

GO:0008876

quinoprotein glucose dehydrogenase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.1.5.2

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0997
UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0037

C

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

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

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. Yamada, M et al. (1998) Mutant isolation of the Escherichia coli quinoprotein glucose dehydrogenase and analysis of crucial residues Asp-730 and His-775 for its function. J. Biol. Chem. 273 22021-7 PubMed GONUTS page
  3. Elias, MD et al. (2004) Occurrence of a bound ubiquinone and its function in Escherichia coli membrane-bound quinoprotein glucose dehydrogenase. J. Biol. Chem. 279 3078-83 PubMed GONUTS page
  4. 4.0 4.1 Yamada, M et al. (1993) Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site. J. Biol. Chem. 268 12812-7 PubMed GONUTS page
  5. James, PL & Anthony, C (2003) The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli. Biochim. Biophys. Acta 1647 200-5 PubMed GONUTS page