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Q8XCJ6 (G6PD_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. 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:Z2904, ECs2562
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [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_0000068119

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
Q8XCJ6 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: FEE38F456F6A7B24

FASTA49155,732
        10         20         30         40         50         60 
MAVTQTAQVC 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]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG56842.1.
BA000007 Genomic DNA. Translation: BAB35985.1.
PIRB90949.
F85797.
RefSeqNP_288289.1. NC_002655.2.
NP_310589.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8XCJ6.
SMRQ8XCJ6. Positions 4-489.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z2904.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG56842; AAG56842; Z2904.
BAB35985; BAB35985; BAB35985.
GeneID912956.
961825.
KEGGece:Z2904.
ecs:ECs2562.
PATRIC18354494. VBIEscCol44059_2458.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0364.
HOGENOMHOG000046191.
KOK00036.
OMADISQKIH.
OrthoDBEOG61308Z.
ProtClustDBPRK05722.

Enzyme and pathway databases

BioCycECOL386585:GJFA-2536-MONOMER.
ECOO157:ZWF-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_ECO57
AccessionPrimary (citable) accession number: Q8XCJ6
Secondary accession number(s): Q7AD71
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 82 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