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P41764 (G6PD_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 97. 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:gsdA
Synonyms:g6pD
ORF Names:AN2981
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length511 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.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentintracellular

Inferred from direct assay PubMed 20797444. Source: ASPGD

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glucose-6-phosphate dehydrogenase activity

Inferred from direct assay PubMed 8277259. Source: ASPGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068103

Regions

Nucleotide binding29 – 368NADP By similarity
Region194 – 1985Substrate binding By similarity

Sites

Active site2561Proton acceptor By similarity
Binding site631NADP By similarity
Binding site1641NADP; via carbonyl oxygen By similarity
Binding site1641Substrate By similarity
Binding site2321Substrate By similarity
Binding site2511Substrate By similarity
Binding site3501Substrate By similarity
Binding site3841Substrate By similarity

Experimental info

Sequence conflict15 – 206Missing in CAA58825. Ref.1
Sequence conflict76 – 8510RSYIKTPTKE → DTLRPRQRK in CAA58825. Ref.1
Sequence conflict3521L → LP in CAA58825. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P41764 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 66BC15B72878A475

FASTA51158,977
        10         20         30         40         50         60 
MSATIARAEE QQNGSTVELK DDTVIVVLGA SGDLAKKKTF PALFGLFRNK FLPKGIKIVG 

        70         80         90        100        110        120 
YARTQMDHNE YLKRVRSYIK TPTKEIEEQL NSFCELCTYI SGQYDQDDSF KNLAKHLEEI 

       130        140        150        160        170        180 
EKNQKEQNRV FYMALPPSVF ITVSEQLKRN CYPKNGVARI IVEKPFGKDL QSSRDLQKAL 

       190        200        210        220        230        240 
EPNWKEEEIF RIDHYLGKEM VKNILIMRFG NEFFNATWNR HHIDNVQITF KEPFGTEGRG 

       250        260        270        280        290        300 
GYFDEFGIIR DVMQNHLLQV LTLLAMERPI SFSAEDIRDE KVRVLRAMDP IQPKDVIIGQ 

       310        320        330        340        350        360 
YGRSLDGSKP AYKEDDTVPQ DSRCPTFCAL VAHIKNERWD GVPFIMKAGK ALNEQKTEIR 

       370        380        390        400        410        420 
IQFKDVTSGI FKDIPRNELV IRVQPNESVY IKMNSKLPGL SMQTVVTELD LTYRRRFSDL 

       430        440        450        460        470        480 
KIPEAYESLI LDALKGDHSN FVRDDELDAS WRMFTPLLHY LDDNKEIIPM EYPYGSRGPS 

       490        500        510 
VLDDFTASYG YKFSDAAGYQ WPLTHTTPNR L 

« Hide

References

« Hide 'large scale' references
[1]Schaap P.J., Muller Y., Visser J.
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]van den Broek P., Goosen T., Wennekes B., van den Broek H.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: WG096.
[3]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[4]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84001 Genomic DNA. Translation: CAA58825.1.
X77830 Genomic DNA. Translation: CAA54841.1.
AACD01000051 Genomic DNA. Translation: EAA63552.1.
BN001306 Genomic DNA. Translation: CBF83624.1.
RefSeqXP_660585.1. XM_655493.1.

3D structure databases

ProteinModelPortalP41764.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP41764.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00010099; CADANIAP00010099; CADANIAG00010099.
GeneID2874290.
KEGGani:AN2981.2.

Phylogenomic databases

eggNOGCOG0364.
HOGENOMHOG000046192.
KOK00036.
OMAAVVFKRA.
OrthoDBEOG7TXKRP.

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_EMENI
AccessionPrimary (citable) accession number: P41764
Secondary accession number(s): C8VIZ3, Q5B8Z9, Q92408
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: February 19, 2014
This is version 97 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

PATHWAY comments

Index of metabolic and biosynthesis pathways