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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

Catalytic activityi

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

Pathway: 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 (Pgd), 6-phosphogluconate dehydrogenase, decarboxylating (Kif1b), 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721NADP 1By similarity
Binding sitei147 – 1471NADP 1By similarity
Binding sitei171 – 1711NADP 1; via carbonyl oxygenBy similarity
Binding sitei171 – 1711SubstrateBy similarity
Binding sitei239 – 2391SubstrateBy similarity
Binding sitei258 – 2581SubstrateBy similarity
Active sitei263 – 2631Proton acceptorBy similarity
Binding sitei357 – 3571NADP 2By similarity
Binding sitei360 – 3601SubstrateBy similarity
Binding sitei365 – 3651SubstrateBy similarity
Binding sitei366 – 3661NADP 2By similarity
Binding sitei370 – 3701NADP 2By similarity
Binding sitei393 – 3931NADP 2By similarity
Binding sitei395 – 3951SubstrateBy similarity
Binding sitei487 – 4871NADP 2By similarity
Binding sitei503 – 5031NADP 2By similarity
Binding sitei509 – 5091NADP 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 458NADP 1By similarity
Nucleotide bindingi401 – 4033NADP 2By similarity
Nucleotide bindingi421 – 4233NADP 2By similarity

GO - Molecular functioni

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

GO - Biological processi

  • cellular response to oxidative stress Source: Ensembl
  • cholesterol biosynthetic process Source: Ensembl
  • cytokine production 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 protein glutathionylation Source: Ensembl
  • pentose biosynthetic process Source: Ensembl
  • pentose-phosphate shunt Source: RGD
  • pentose-phosphate shunt, oxidative branch Source: RGD
  • regulation of neuron apoptotic process Source: RGD
  • response to ethanol Source: RGD
  • response to food Source: RGD
  • response to organic cyclic compound Source: RGD
  • ribose phosphate biosynthetic process Source: Ensembl
  • substantia nigra development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_281325. Pentose phosphate pathway (hexose monophosphate shunt).
REACT_358301. TP53 Regulates Metabolic Genes.
SABIO-RKP05370.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2645. G6pdx.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: Ensembl
  • cytoplasmic side of plasma membrane Source: Ensembl
  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • intracellular membrane-bounded organelle Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 515514Glucose-6-phosphate 1-dehydrogenasePRO_0000068087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei89 – 891N6-acetyllysineBy similarity
Modified residuei171 – 1711N6-acetyllysineBy similarity
Modified residuei403 – 4031N6-acetyllysineBy similarity
Modified residuei432 – 4321N6-acetyllysineBy similarity
Modified residuei497 – 4971N6-acetyllysineBy similarity

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

Proteomic databases

PaxDbiP05370.
PRIDEiP05370.

2D gel databases

World-2DPAGE0004:P05370.

PTM databases

PhosphoSiteiP05370.

Expressioni

Gene expression databases

GenevisibleiP05370. RN.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000053157.

Structurei

3D structure databases

ProteinModelPortaliP05370.
SMRiP05370. Positions 28-515.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 2055Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0364.
GeneTreeiENSGT00530000063435.
HOGENOMiHOG000046192.
HOVERGENiHBG000856.
InParanoidiP05370.
KOiK00036.
OMAiHNLQTTK.
OrthoDBiEOG7DRJ2T.
PhylomeDBiP05370.
TreeFamiTF300584.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00966. G6PD.
InterProiIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000110. G6PD. 1 hit.
PRINTSiPR00079. G6PDHDRGNASE.
TIGRFAMsiTIGR00871. zwf. 1 hit.
PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti320 – 3201N → D AA sequence (PubMed:2606104).Curated

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

EnsembliENSRNOT00000056317; ENSRNOP00000053157; ENSRNOG00000037254.
GeneIDi24377.
KEGGirno:24377.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP05370.
SMRiP05370. Positions 28-515.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000053157.

PTM databases

PhosphoSiteiP05370.

2D gel databases

World-2DPAGE0004:P05370.

Proteomic databases

PaxDbiP05370.
PRIDEiP05370.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000056317; ENSRNOP00000053157; ENSRNOG00000037254.
GeneIDi24377.
KEGGirno:24377.

Organism-specific databases

CTDi2539.
RGDi2645. G6pdx.

Phylogenomic databases

eggNOGiCOG0364.
GeneTreeiENSGT00530000063435.
HOGENOMiHOG000046192.
HOVERGENiHBG000856.
InParanoidiP05370.
KOiK00036.
OMAiHNLQTTK.
OrthoDBiEOG7DRJ2T.
PhylomeDBiP05370.
TreeFamiTF300584.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00408.
ReactomeiREACT_281325. Pentose phosphate pathway (hexose monophosphate shunt).
REACT_358301. TP53 Regulates Metabolic Genes.
SABIO-RKP05370.

Miscellaneous databases

NextBioi603131.
PROiP05370.

Gene expression databases

GenevisibleiP05370. RN.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00966. G6PD.
InterProiIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000110. G6PD. 1 hit.
PRINTSiPR00079. G6PDHDRGNASE.
TIGRFAMsiTIGR00871. zwf. 1 hit.
PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
    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.

Entry informationi

Entry nameiG6PD_RAT
AccessioniPrimary (citable) accession number: P05370
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.