Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0AC54 (G6PD_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-6-phosphate 1-dehydrogenase

Short name=G6PD
EC=1.1.1.49
Gene names
Name:zwf
Ordered Locus Names:c2265
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone By similarity. HAMAP-Rule MF_00966

Catalytic activity

D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH. HAMAP-Rule MF_00966

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. HAMAP-Rule MF_00966

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glucose-6-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068120

Regions

Nucleotide binding92 – 932NADP By similarity

Sites

Active site2391Proton acceptor By similarity
Binding site501NADP By similarity
Binding site1471NADP By similarity
Binding site1771Substrate By similarity
Binding site1811Substrate By similarity
Binding site2151Substrate By similarity
Binding site2341Substrate By similarity
Binding site3391Substrate By similarity
Binding site3441Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AC54 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 263F07D298EAFCD3

FASTA49155,704
        10         20         30         40         50         60 
MAVTQTAQAC DLVIFGAKGD LARRKLLPSL YQLEKAGQLN PDTRIIGVGR ADWDKAAYTK 

        70         80         90        100        110        120 
VVREALETFM KETIDEGLWD TLSARLDFCN LDVNDTAAFS RLGAMLDQKN RITINYFAMP 

       130        140        150        160        170        180 
PSTFGAICKG LGEAKLNAKP ARVVMEKPLG TSLATSQEIN DQVGEYFEEC QVYRIDHYLG 

       190        200        210        220        230        240 
KETVLNLLAL RFANSLFVNN WDNRTIDHVE ITVAEEVGIE GRWGYFDKAG QMRDMIQNHL 

       250        260        270        280        290        300 
LQILCMIAMS PPSDLSADSI RDEKVKVLKS LRRIDRSNVR EKTVRGQYTA GFAQGKKVPG 

       310        320        330        340        350        360 
YLEEEGANKS SNTETFVAIR VDIDNWRWAG VPFYLRTGKR LPTKCSEVVV YFKTPELNLF 

       370        380        390        400        410        420 
KESWQDLPQN KLTIRLQPDE GVDIQVLNKV PGLDHKHNLQ ITKLDLSYSE TFNQTHLADA 

       430        440        450        460        470        480 
YERLLLETMR GIQALFVRRD EVEEAWKWVD SITEAWAMDN DAPKPYQAGT WGPVASVAMI 

       490 
TRDGRSWNEF E 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN80722.1.
RefSeqNP_754157.1. NC_004431.1.

3D structure databases

ProteinModelPortalP0AC54.
SMRP0AC54. Positions 8-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c2265.

Proteomic databases

PRIDEP0AC54.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN80722; AAN80722; c2265.
GeneID1036807.
KEGGecc:c2265.
PATRIC18282411. VBIEscCol75197_2122.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000046191.
KOK00036.
OMADISQKIH.
OrthoDBEOG61308Z.
ProtClustDBPRK05722.

Enzyme and pathway databases

BioCycECOL199310:C2265-MONOMER.
UniPathwayUPA00115; UER00408.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00966. G6PD.
InterProIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23429. PTHR23429. 1 hit.
PfamPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFPIRSF000110. G6PD. 1 hit.
PRINTSPR00079. G6PDHDRGNASE.
TIGRFAMsTIGR00871. zwf. 1 hit.
PROSITEPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG6PD_ECOL6
AccessionPrimary (citable) accession number: P0AC54
Secondary accession number(s): P22992 expand/collapse secondary AC list , P78069, Q60134, Q60139
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: March 19, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways