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Protein

Glucose-6-phosphate 1-dehydrogenase

Gene

G6pdx

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Miscellaneous

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

Catalytic activityi

D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH.

Pathwayi: pentose phosphate pathway

This protein is involved in step 1 of the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glucose-6-phosphate 1-dehydrogenase (G6pdx)
  2. 6-phosphogluconolactonase (Pgls)
  3. 6-phosphogluconate dehydrogenase, decarboxylating (Kif1b), 6-phosphogluconate dehydrogenase, decarboxylating (Pgd), 6-phosphogluconate dehydrogenase, decarboxylating (Pgd)
This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei72NADP 1By similarity1
Binding sitei147NADP 1By similarity1
Binding sitei171NADP 1; via carbonyl oxygenBy similarity1
Binding sitei171SubstrateBy similarity1
Binding sitei239SubstrateBy similarity1
Binding sitei258SubstrateBy similarity1
Active sitei263Proton acceptorBy similarity1
Binding sitei357NADP 2By similarity1
Binding sitei360SubstrateBy similarity1
Binding sitei365SubstrateBy similarity1
Binding sitei366NADP 2By similarity1
Binding sitei370NADP 2By similarity1
Binding sitei393NADP 2By similarity1
Binding sitei395SubstrateBy similarity1
Binding sitei487NADP 2By similarity1
Binding sitei503NADP 2By similarity1
Binding sitei509NADP 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi38 – 45NADP 1By similarity8
Nucleotide bindingi401 – 403NADP 2By similarity3
Nucleotide bindingi421 – 423NADP 2By similarity3

GO - Molecular functioni

  • carbohydrate binding Source: RGD
  • glucose-6-phosphate dehydrogenase activity Source: CACAO
  • glucose binding Source: RGD
  • NADP binding Source: RGD
  • protein homodimerization activity Source: Ensembl

GO - Biological processi

  • cellular response to oxidative stress Source: Ensembl
  • cholesterol biosynthetic process Source: Ensembl
  • erythrocyte maturation Source: Ensembl
  • glucose 6-phosphate metabolic process Source: RGD
  • glucose metabolic process Source: UniProtKB-KW
  • glutathione metabolic process Source: Ensembl
  • NADPH regeneration Source: Ensembl
  • NADP metabolic process Source: UniProtKB
  • negative regulation of cell growth involved in cardiac muscle cell development Source: RGD
  • negative regulation of protein glutathionylation Source: Ensembl
  • negative regulation of reactive oxygen species metabolic process Source: RGD
  • pentose biosynthetic process Source: Ensembl
  • pentose-phosphate shunt Source: RGD
  • pentose-phosphate shunt, oxidative branch Source: RGD
  • positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel Source: RGD
  • regulation of neuron apoptotic process Source: RGD
  • response to ethanol Source: RGD
  • response to food Source: RGD
  • response to iron(III) ion Source: RGD
  • response to organic cyclic compound Source: RGD
  • ribose phosphate biosynthetic process Source: Ensembl
  • substantia nigra development Source: Ensembl

Keywordsi

Molecular functionOxidoreductase
Biological processCarbohydrate metabolism, Glucose metabolism
LigandNADP

Enzyme and pathway databases

ReactomeiR-RNO-5628897. TP53 Regulates Metabolic Genes.
R-RNO-71336. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RKiP05370.
UniPathwayiUPA00115; UER00408.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate 1-dehydrogenase (EC:1.1.1.49)
Short name:
G6PD
Gene namesi
Name:G6pdx
Synonyms:G6pd
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi2645. G6pdx.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic side of plasma membrane Source: Ensembl
  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • intracellular membrane-bounded organelle Source: RGD
  • nucleus Source: RGD

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000680872 – 515Glucose-6-phosphate 1-dehydrogenaseAdd BLAST514

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei8PhosphoserineBy similarity1
Modified residuei10PhosphothreonineBy similarity1
Modified residuei89N6-acetyllysineBy similarity1
Modified residuei171N6-acetyllysineBy similarity1
Modified residuei403N6-acetyllysineBy similarity1
Modified residuei432N6-acetyllysineBy similarity1
Modified residuei497N6-acetyllysineBy similarity1
Modified residuei503PhosphotyrosineBy similarity1

Post-translational modificationi

Acetylated by ELP3 at Lys-403; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403; deacetylation stimulates its enzyme activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP05370.
PRIDEiP05370.

2D gel databases

World-2DPAGEi0004:P05370.

PTM databases

iPTMnetiP05370.
PhosphoSitePlusiP05370.

Expressioni

Gene expression databases

BgeeiENSRNOG00000056728.
GenevisibleiP05370. RN.

Interactioni

Subunit structurei

Homotetramer; dimer of dimers. Interacts with SIRT2; the interaction is enhanced by H2O2 treatment (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi246548. 1 interactor.
STRINGi10116.ENSRNOP00000053157.

Structurei

3D structure databases

ProteinModelPortaliP05370.
SMRiP05370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni201 – 205Substrate bindingBy similarity5

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0563. Eukaryota.
COG0364. LUCA.
GeneTreeiENSGT00530000063435.
HOGENOMiHOG000046192.
HOVERGENiHBG000856.
InParanoidiP05370.
KOiK00036.
OMAiVEICVYE.
OrthoDBiEOG091G06FN.
PhylomeDBiP05370.
TreeFamiTF300584.

Family and domain databases

HAMAPiMF_00966. G6PD. 1 hit.
InterProiView protein in InterPro
IPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiView protein in Pfam
PF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
PIRSFiPIRSF000110. G6PD. 1 hit.
PRINTSiPR00079. G6PDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00871. zwf. 1 hit.
PROSITEiView protein in PROSITE
PS00069. G6P_DEHYDROGENASE. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05370-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEQVALSRT QVCGILREEL YQGDAFHQAD THIFIIMGAS GDLAKKKIYP
60 70 80 90 100
TIWWLFRDGL LPEDTFIVGY ARSRLTVDDI RKQSEPFFKV TPEERPKLEE
110 120 130 140 150
FFARNSYVAG QYDDPASYKH LNSHMNALHQ GMQANRLFYL ALPPTVYEAV
160 170 180 190 200
TKNIQEICMS QTGWNRIIVE KPFGRDLQSS NQLSNHISSL FREDQIYRID
210 220 230 240 250
HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP FGTEGRGGYF
260 270 280 290 300
DEFGIIRDVM QNHLLQMLCL VAMEKPASTD SDDVRDEKVK VLKCISEVET
310 320 330 340 350
DNVVLGQYVG NPSGEGEATN GYLDDPTVPH GSTTATFAAA VLYVENERWD
360 370 380 390 400
GVPFILRCGK ALNERKAEVR LQFRDVAGDI FHQQCKRNEL VIRVQPNEAV
410 420 430 440 450
YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM
460 470 480 490 500
HFVRSDELRE AWRIFTPLLH KIDREKPQPI PYVYGSRGPT EADELMKRVG
510
FQYEGTYKWV NPHKL
Length:515
Mass (Da):59,376
Last modified:January 23, 2007 - v3
Checksum:i8E92FFF3BF5A959B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti320N → D AA sequence (PubMed:2606104).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07467 mRNA. Translation: CAA30355.1.
BC081820 mRNA. Translation: AAH81820.1.
M26655, M26653, M26654 Genomic DNA. Translation: AAA41179.1.
PIRiS01233.
RefSeqiNP_058702.1. NM_017006.2.
UniGeneiRn.11040.

Genome annotation databases

EnsembliENSRNOT00000080887; ENSRNOP00000075297; ENSRNOG00000056728.
GeneIDi24377.
KEGGirno:24377.

Similar proteinsi

Entry informationi

Entry nameiG6PD_RAT
AccessioniPrimary (citable) accession number: P05370
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 159 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families