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P05370

- G6PD_RAT

UniProt

P05370 - G6PD_RAT

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Protein
Glucose-6-phosphate 1-dehydrogenase
Gene
G6pdx, G6pd
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721NADP 1 By similarity
Binding sitei147 – 1471NADP 1 By similarity
Binding sitei171 – 1711NADP 1; via carbonyl oxygen By similarity
Binding sitei171 – 1711Substrate By similarity
Binding sitei239 – 2391Substrate By similarity
Binding sitei258 – 2581Substrate By similarity
Active sitei263 – 2631Proton acceptor By similarity
Binding sitei357 – 3571NADP 2 By similarity
Binding sitei360 – 3601Substrate By similarity
Binding sitei365 – 3651Substrate By similarity
Binding sitei366 – 3661NADP 2 By similarity
Binding sitei370 – 3701NADP 2 By similarity
Binding sitei393 – 3931NADP 2 By similarity
Binding sitei395 – 3951Substrate By similarity
Binding sitei487 – 4871NADP 2 By similarity
Binding sitei503 – 5031NADP 2 By similarity
Binding sitei509 – 5091NADP 2 By similarity

Regions

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

GO - Molecular functioni

  1. NADP binding Source: RGD
  2. carbohydrate binding Source: RGD
  3. glucose binding Source: RGD
  4. glucose-6-phosphate dehydrogenase activity Source: RGD

GO - Biological processi

  1. NADP metabolic process Source: UniProtKB
  2. cellular response to oxidative stress Source: Ensembl
  3. cholesterol biosynthetic process Source: Ensembl
  4. cytokine production Source: Ensembl
  5. erythrocyte maturation Source: Ensembl
  6. glucose 6-phosphate metabolic process Source: RGD
  7. glutathione metabolic process Source: Ensembl
  8. negative regulation of protein glutathionylation Source: Ensembl
  9. pentose biosynthetic process Source: Ensembl
  10. pentose-phosphate shunt Source: RGD
  11. pentose-phosphate shunt, oxidative branch Source: RGD
  12. regulation of neuron apoptotic process Source: RGD
  13. response to ethanol Source: RGD
  14. response to food Source: RGD
  15. response to organic cyclic compound Source: RGD
  16. ribose phosphate biosynthetic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_226758. Pentose phosphate pathway (hexose monophosphate shunt).
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: Chromosome 1

Organism-specific databases

RGDi2645. G6pdx.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: Ensembl
  2. cytoplasmic side of plasma membrane Source: Ensembl
  3. cytosol Source: RGD
  4. intracellular membrane-bounded organelle Source: RGD
  5. nucleus Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 515514Glucose-6-phosphate 1-dehydrogenase
PRO_0000068087Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP05370.
PRIDEiP05370.

2D gel databases

World-2DPAGE0004:P05370.

PTM databases

PhosphoSiteiP05370.

Expressioni

Gene expression databases

GenevestigatoriP05370.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000053157.

Structurei

3D structure databases

ProteinModelPortaliP05370.
SMRiP05370. Positions 28-515.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0364.
GeneTreeiENSGT00530000063435.
HOGENOMiHOG000046192.
HOVERGENiHBG000856.
InParanoidiP05370.
KOiK00036.
OMAiKLQPIPY.
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

MAEQVALSRT QVCGILREEL YQGDAFHQAD THIFIIMGAS GDLAKKKIYP    50
TIWWLFRDGL LPEDTFIVGY ARSRLTVDDI RKQSEPFFKV TPEERPKLEE 100
FFARNSYVAG QYDDPASYKH LNSHMNALHQ GMQANRLFYL ALPPTVYEAV 150
TKNIQEICMS QTGWNRIIVE KPFGRDLQSS NQLSNHISSL FREDQIYRID 200
HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP FGTEGRGGYF 250
DEFGIIRDVM QNHLLQMLCL VAMEKPASTD SDDVRDEKVK VLKCISEVET 300
DNVVLGQYVG NPSGEGEATN GYLDDPTVPH GSTTATFAAA VLYVENERWD 350
GVPFILRCGK ALNERKAEVR LQFRDVAGDI FHQQCKRNEL VIRVQPNEAV 400
YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM 450
HFVRSDELRE AWRIFTPLLH KIDREKPQPI PYVYGSRGPT EADELMKRVG 500
FQYEGTYKWV NPHKL 515
Length:515
Mass (Da):59,376
Last modified:January 23, 2007 - v3
Checksum:i8E92FFF3BF5A959B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti320 – 3201N → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X07467 mRNA. Translation: CAA30355.1 .
BC081820 mRNA. Translation: AAH81820.1 .
M26655 , M26653 , M26654 Genomic DNA. Translation: AAA41179.1 .
PIRi S01233.
RefSeqi NP_058702.1. NM_017006.2.
UniGenei Rn.11040.

3D structure databases

ProteinModelPortali P05370.
SMRi P05370. Positions 28-515.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000053157.

PTM databases

PhosphoSitei P05370.

2D gel databases

World-2DPAGE 0004:P05370.

Proteomic databases

PaxDbi P05370.
PRIDEi P05370.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000056317 ; ENSRNOP00000053157 ; ENSRNOG00000037254 .
GeneIDi 24377.
KEGGi rno:24377.

Organism-specific databases

CTDi 2539.
RGDi 2645. G6pdx.

Phylogenomic databases

eggNOGi COG0364.
GeneTreei ENSGT00530000063435.
HOGENOMi HOG000046192.
HOVERGENi HBG000856.
InParanoidi P05370.
KOi K00036.
OMAi KLQPIPY.
OrthoDBi EOG7DRJ2T.
PhylomeDBi P05370.
TreeFami TF300584.

Enzyme and pathway databases

UniPathwayi UPA00115 ; UER00408 .
Reactomei REACT_226758. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RK P05370.

Miscellaneous databases

NextBioi 603131.

Gene expression databases

Genevestigatori P05370.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00966. G6PD.
InterProi IPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR23429. PTHR23429. 1 hit.
Pfami PF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000110. G6PD. 1 hit.
PRINTSi PR00079. G6PDHDRGNASE.
TIGRFAMsi TIGR00871. zwf. 1 hit.
PROSITEi PS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 133 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

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