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

O00091 (G6PD_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:zwf1
ORF Names:SPAC3A12.18, SPAC9.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068106

Regions

Nucleotide binding18 – 258NADP By similarity
Region185 – 1895Substrate binding By similarity

Sites

Active site2471Proton acceptor By similarity
Binding site521NADP By similarity
Binding site1551NADP; via carbonyl oxygen By similarity
Binding site1551Substrate By similarity
Binding site2231Substrate By similarity
Binding site2421Substrate By similarity
Binding site3411Substrate By similarity
Binding site3751Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O00091 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 6706DD0847762A22

FASTA50057,204
        10         20         30         40         50         60 
MSSANLSIKE NGAMVVFGAS GDLSKKKTFP ALFSLFSEGR LPKDIRIVGY ARSKIEHEDF 

        70         80         90        100        110        120 
LDRITQNIKI DEEDSQAKEK LEEFKKRCSY YRGSYDKPED FEGLNSHLCE REGDRSTHNR 

       130        140        150        160        170        180 
IFYLALPPDV FVSVATNLKK KCVPEKGIAR LVIEKPFGVD LKSAQELQSQ LAPLFDEKEI 

       190        200        210        220        230        240 
YRIDHYLGKE MVQNLVHLRF CNPVISHLWD KNSISSVQIT FKEPIGTEGR GGYFDSSTIV 

       250        260        270        280        290        300 
RDIVQNHLVQ ILTLLTMETP TTFSADDLRD EKVKVLRRTR LGDLKDIVLG QYVKSKDGKK 

       310        320        330        340        350        360 
PGYLDDETVP KGSRCPTYSA IPCFIDTERW RGVPFLLKAG KAMDIGKVEI RVQFKAAANG 

       370        380        390        400        410        420 
LFKDAYHNEL VIRVQPDEAI YFKMNIKQPG LSEAPLLTDL DLTYSRRFKN MKLHEAYEAL 

       430        440        450        460        470        480 
FLDAFAGDQS RFARIDELEC AWSLVDPLLK YMEEEKPVPE PYEYGSDGPE CLYSFLKKFG 

       490        500 
YIYDSPDYYD YPVMSVPSDH 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB08746.1.
PIRT39186.
RefSeqNP_593344.2. NM_001018776.2.

3D structure databases

ProteinModelPortalO00091.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279629. 4 interactions.
IntActO00091. 1 interaction.
MINTMINT-4666413.
STRING4896.SPAC3A12.18-1.

Proteomic databases

MaxQBO00091.
PaxDbO00091.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC3A12.18.1; SPAC3A12.18.1:pep; SPAC3A12.18.
GeneID2543200.
KEGGspo:SPAC3A12.18.

Organism-specific databases

PomBaseSPAC3A12.18.

Phylogenomic databases

eggNOGCOG0364.
HOGENOMHOG000046192.
KOK00036.
OMAYEIQEAN.
OrthoDBEOG7TXKRP.
PhylomeDBO00091.

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...

Other

NextBio20804223.
PROO00091.

Entry information

Entry nameG6PD_SCHPO
AccessionPrimary (citable) accession number: O00091
Secondary accession number(s): Q9UT26
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: May 14, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways