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P48828 (G6PD_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 95. 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:KLLA0D19855g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length497 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
Gene Ontology (GO)
   Biological_processpentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glucose-6-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 497497Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068104

Regions

Nucleotide binding15 – 228NADP By similarity
Region183 – 1875Substrate binding By similarity

Sites

Active site2451Proton acceptor By similarity
Binding site491NADP By similarity
Binding site1531NADP; via carbonyl oxygen By similarity
Binding site1531Substrate By similarity
Binding site2211Substrate By similarity
Binding site2401Substrate By similarity
Binding site3391Substrate By similarity
Binding site3731Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P48828 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: C6EC57AD6B6E9F1F

FASTA49756,574
        10         20         30         40         50         60 
MATQFDENTV ITIFGASGDL SKKKTFPALF GLYREGYLNP TTKIIGYARS KLSNEDLREK 

        70         80         90        100        110        120 
VKPFLKKPNG AKDDAKVNEF LSMVSYHAGP YDSDEGYLEL KKIIEEFEAE KKVDEPHRLF 

       130        140        150        160        170        180 
YLALPPSIFI DVCSKLKENL YTESGIQRVI VEKPFGHDLQ SATELQEKLA PLFSEDELFR 

       190        200        210        220        230        240 
IDHYLGKEMV KNLLLMRFGN TFLNAAWNKE NIQSVQVVFK EPFGTEGRGG YFDSIGIIRD 

       250        260        270        280        290        300 
VMQNHLLQVL TLLTMERPVS FDPESVRDEK VKVLKAFSPI DHDDILIGQY GRSVDGSKPS 

       310        320        330        340        350        360 
YLDDETVKED SKCVTFAAIG FKIANERWDG VPIVMRAGKA LNEGKVEIRI QFRRVASGMF 

       370        380        390        400        410        420 
TDIPNNELVI RIQPNEAIYL KCNAKTPGLA NENQTTELDL TYSERYKNYW IPEAYESLIR 

       430        440        450        460        470        480 
DALLGDHSNF VRDDELDVSW KLFTPLLNYL EGPDGPQPKI YPYGCRSPDG LVEFLADHGY 

       490 
TFSKPGSYQW PVTTPKM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70373 Genomic DNA. Translation: CAA49834.1.
CR382124 Genomic DNA. Translation: CAH01040.1.
PIRS31337.
RefSeqXP_453944.1. XM_453944.1.

3D structure databases

ProteinModelPortalP48828.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.P48828.

Proteomic databases

PRIDEP48828.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2893289.
KEGGkla:KLLA0D19855g.

Phylogenomic databases

eggNOGCOG0364.
HOGENOMHOG000046192.
KOK00036.
OMAYCVTAVS.
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_KLULA
AccessionPrimary (citable) accession number: P48828
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 14, 2014
This is version 95 of the entry and version 1 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