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P77809 (G6PD_AGGAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. 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
OrganismAggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans)
Taxonomic identifier714 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeAggregatibacter

Protein attributes

Sequence length494 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
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 – 494494Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068108

Sites

Active site2421Proton acceptor By similarity
Binding site461NADP By similarity
Binding site1501NADP By similarity
Binding site1801Substrate By similarity
Binding site1841Substrate By similarity
Binding site2181Substrate By similarity
Binding site2371Substrate By similarity
Binding site3421Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P77809 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: B0B2A32F349936A2

FASTA49456,385
        10         20         30         40         50         60 
MKAENCCIVI FGASGDLTYR KLIPALYNLY KIDRLGEDFS VLGVARTELN DKSFREKMRQ 

        70         80         90        100        110        120 
TLIKNEGAKG ECLEQFCSHL YYQAVNTADK ADYAKLVPRL DELHDTYRTE GNTLYYLSTP 

       130        140        150        160        170        180 
PSLYGVIPEC LGEHGLNKED RGWKRLIVEK PFGYDRETAE ALDIQIHRFF EEHQIYRIDH 

       190        200        210        220        230        240 
YLGKETVQNL LVLRFSNGWF EPLWNRNFID YIEITGAESI GVEERGGYYD GSGAMRDMFQ 

       250        260        270        280        290        300 
NHLLQVLAMV AMEPPVIINA NSMRDEVAKV LHCLRPLTQE DVEHNLVLGQ YVAGEVDGEW 

       310        320        330        340        350        360 
VKGYLEEKGV PPYSTTETYM ALRCEIENWR WAGVPFYVRT GKRLPARVTE IVIHFKTTPH 

       370        380        390        400        410        420 
PVFSQNAPEN KLIIRIQPDE GISMRFGLKK PGAGFEAKEV SMDFRYADLA GATVMTAYER 

       430        440        450        460        470        480 
LLLDAMKGDA TLFARTDAVH AAWKFVQPIL NYKAQGGRLY DYEAGTWGPT AADKLIAKSG 

       490 
RVWRRPSGLM KKKV 

« Hide

References

[1]"The gnd gene encoding a novel 6-phosphogluconate dehydrogenase and its adjacent region of Actinobacillus actinomycetemcomitans chromosomal DNA."
Yoshida Y., Nakano Y., Yamashita Y., Koga T.
Biochem. Biophys. Res. Commun. 230:220-225(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43718 / FDC Y4 / Serotype b.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D88189 Genomic DNA. Translation: BAA13554.1.

3D structure databases

ProteinModelPortalP77809.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP77809.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_AGGAC
AccessionPrimary (citable) accession number: P77809
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: February 19, 2014
This is version 76 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