Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P05370

- G6PD_RAT

UniProt

P05370 - G6PD_RAT

Protein

Glucose-6-phosphate 1-dehydrogenase

Gene

G6pdx

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    Pathwayi

    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

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

    GO - Biological processi

    1. cellular response to oxidative stress Source: Ensembl
    2. cholesterol biosynthetic process Source: Ensembl
    3. cytokine production Source: Ensembl
    4. erythrocyte maturation Source: Ensembl
    5. glucose 6-phosphate metabolic process Source: RGD
    6. glutathione metabolic process Source: Ensembl
    7. NADP metabolic process Source: UniProtKB
    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

    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

    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

    GenevestigatoriP05370.

    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.
    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 134 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