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P05370 (G6PD_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. 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:G6pdx
Synonyms:G6pd
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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

Subunit structure

Homotetramer; dimer of dimers By similarity. HAMAP-Rule MF_00966

Miscellaneous

Has NADP both as cofactor (bound to the N-terminal domain) and as structural element bound to the C-terminal domain.

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNADP metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

cholesterol biosynthetic process

Inferred from electronic annotation. Source: Ensembl

cytokine production

Inferred from electronic annotation. Source: Ensembl

erythrocyte maturation

Inferred from electronic annotation. Source: Ensembl

glucose 6-phosphate metabolic process

Inferred from direct assay PubMed 17447164. Source: RGD

glutathione metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein glutathionylation

Inferred from electronic annotation. Source: Ensembl

pentose biosynthetic process

Inferred from electronic annotation. Source: Ensembl

pentose-phosphate shunt

Inferred from direct assay PubMed 2843500. Source: RGD

pentose-phosphate shunt, oxidative branch

Inferred from mutant phenotype PubMed 9794092. Source: RGD

regulation of neuron apoptotic process

Inferred from direct assay PubMed 12414804. Source: RGD

response to ethanol

Inferred from direct assay PubMed 18488910. Source: RGD

response to food

Inferred from expression pattern PubMed 19076169. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 17250641. Source: RGD

ribose phosphate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasmic side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from direct assay PubMed 1834654. Source: RGD

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 2843500. Source: RGD

nucleus

Inferred from direct assay PubMed 15942958. Source: RGD

   Molecular_functionNADP binding

Inferred from direct assay PubMed 17447164. Source: RGD

carbohydrate binding

Inferred from direct assay PubMed 2843500. Source: RGD

glucose binding

Inferred from direct assay PubMed 17447164. Source: RGD

glucose-6-phosphate dehydrogenase activity

Inferred from direct assay PubMed 11735100PubMed 17447164PubMed 18062843PubMed 1834654PubMed 2843500. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 515514Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068087

Regions

Nucleotide binding38 – 458NADP 1 By similarity
Nucleotide binding401 – 4033NADP 2 By similarity
Nucleotide binding421 – 4233NADP 2 By similarity
Region201 – 2055Substrate binding By similarity

Sites

Active site2631Proton acceptor By similarity
Binding site721NADP 1 By similarity
Binding site1471NADP 1 By similarity
Binding site1711NADP 1; via carbonyl oxygen By similarity
Binding site1711Substrate By similarity
Binding site2391Substrate By similarity
Binding site2581Substrate By similarity
Binding site3571NADP 2 By similarity
Binding site3601Substrate By similarity
Binding site3651Substrate By similarity
Binding site3661NADP 2 By similarity
Binding site3701NADP 2 By similarity
Binding site3931NADP 2 By similarity
Binding site3951Substrate By similarity
Binding site4871NADP 2 By similarity
Binding site5031NADP 2 By similarity
Binding site5091NADP 2 By similarity

Amino acid modifications

Modified residue21N-acetylalanine HAMAP-Rule MF_00966
Modified residue891N6-acetyllysine By similarity
Modified residue1711N6-acetyllysine By similarity
Modified residue4031N6-acetyllysine By similarity
Modified residue4321N6-acetyllysine By similarity
Modified residue4971N6-acetyllysine By similarity

Experimental info

Sequence conflict3201N → D AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P05370 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8E92FFF3BF5A959B

FASTA51559,376
        10         20         30         40         50         60 
MAEQVALSRT QVCGILREEL YQGDAFHQAD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL 

        70         80         90        100        110        120 
LPEDTFIVGY ARSRLTVDDI RKQSEPFFKV TPEERPKLEE FFARNSYVAG QYDDPASYKH 

       130        140        150        160        170        180 
LNSHMNALHQ GMQANRLFYL ALPPTVYEAV TKNIQEICMS QTGWNRIIVE KPFGRDLQSS 

       190        200        210        220        230        240 
NQLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP 

       250        260        270        280        290        300 
FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTD SDDVRDEKVK VLKCISEVET 

       310        320        330        340        350        360 
DNVVLGQYVG NPSGEGEATN GYLDDPTVPH GSTTATFAAA VLYVENERWD GVPFILRCGK 

       370        380        390        400        410        420 
ALNERKAEVR LQFRDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL 

       430        440        450        460        470        480 
DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH KIDREKPQPI 

       490        500        510 
PYVYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence of a cDNA encoding rat glucose-6-phosphate dehydrogenase."
Ho Y., Howard A.J., Crapo J.D.
Nucleic Acids Res. 16:7746-7746(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]"Glucose-6-phosphate dehydrogenase. Characteristics revealed by the rat liver enzyme structure."
Jeffery J., Barros-Soederling J., Murray L., Wood I., Hansen R., Szepesi B., Joernvall H.
Eur. J. Biochem. 186:551-556(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-514.
Strain: Wistar.
Tissue: Liver.
[4]Fritz R.S., Kletzien R.F.
Submitted (NOV-1989) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-515.
[5]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 58-72; 176-192 AND 228-257, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07467 mRNA. Translation: CAA30355.1.
BC081820 mRNA. Translation: AAH81820.1.
M26655, M26653, M26654 Genomic DNA. Translation: AAA41179.1.
PIRS01233.
RefSeqNP_058702.1. NM_017006.2.
UniGeneRn.11040.

3D structure databases

ProteinModelPortalP05370.
SMRP05370. Positions 28-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000053157.

PTM databases

PhosphoSiteP05370.

2D gel databases

World-2DPAGE0004:P05370.

Proteomic databases

PaxDbP05370.
PRIDEP05370.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000056317; ENSRNOP00000053157; ENSRNOG00000037254.
GeneID24377.
KEGGrno:24377.

Organism-specific databases

CTD2539.
RGD2645. G6pdx.

Phylogenomic databases

eggNOGCOG0364.
GeneTreeENSGT00530000063435.
HOGENOMHOG000046192.
HOVERGENHBG000856.
InParanoidP05370.
KOK00036.
OMAAVVFKRA.
OrthoDBEOG7DRJ2T.
PhylomeDBP05370.
TreeFamTF300584.

Enzyme and pathway databases

SABIO-RKP05370.
UniPathwayUPA00115; UER00408.

Gene expression databases

GenevestigatorP05370.

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

NextBio603131.

Entry information

Entry nameG6PD_RAT
AccessionPrimary (citable) accession number: P05370
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways