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O55044

- G6PD_CRIGR

UniProt

O55044 - G6PD_CRIGR

Protein

Glucose-6-phosphate 1-dehydrogenase

Gene

G6PD

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. glucose-6-phosphate dehydrogenase activity Source: UniProtKB
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. glucose 6-phosphate metabolic process Source: UniProtKB
    2. NADP metabolic process Source: UniProtKB
    3. pentose-phosphate shunt Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00115; UER00408.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucose-6-phosphate 1-dehydrogenase (EC:1.1.1.49)
    Short name:
    G6PD
    Gene namesi
    Name:G6PD
    OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
    Taxonomic identifieri10029 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 515514Glucose-6-phosphate 1-dehydrogenasePRO_0000068081Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    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

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliO55044.
    SMRiO55044. Positions 28-515.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG000856.
    KOiK00036.

    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.

    O55044-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEQVALSRT QVCGILREEL YQGDAFHQAD THIFIIMGAS GDLAKKKIYP    50
    TIWWLFRDGL LPEDTFIVGY ARSRLTVDDI RKQSEPFFKA TPEERPKLEE 100
    FFARNSYVAG QYDDPASYKH LNSHMNALHQ GMQANRLFYL ALPPTVYEAV 150
    TKNIQETCMS QTGWNRIIVE KPFGRDLQSS NQLSNHISSL FREDQIYRID 200
    HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP FGTEGRGGYF 250
    DEFGIIRDVM QNHLLQMLCL VAMEKPASTD SDDVRDEKVK VLKCISEVET 300
    SNVVLGQYVG NPNGEGEATN GYLDDPTVPR GSTTATFAAA VLYVENERWD 350
    GVPFILRCGK ALNERKAEVR LQFRDVAGDI FHQQCKRNEL VIRVQPNEAV 400
    YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM 450
    HFVRSDELRE AWRIFTPLLH KIDQEKPQPI PYVYGSRGPT EADELMKRVG 500
    FQYEGTYKWV NPHKL 515
    Length:515
    Mass (Da):59,326
    Last modified:January 23, 2007 - v3
    Checksum:i892DD70C86C7438C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF044676 mRNA. Translation: AAC00204.1.
    RefSeqiNP_001233656.1. NM_001246727.1.

    Genome annotation databases

    GeneIDi100689469.
    KEGGicge:100689469.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF044676 mRNA. Translation: AAC00204.1 .
    RefSeqi NP_001233656.1. NM_001246727.1.

    3D structure databases

    ProteinModelPortali O55044.
    SMRi O55044. Positions 28-515.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100689469.
    KEGGi cge:100689469.

    Organism-specific databases

    CTDi 2539.

    Phylogenomic databases

    HOVERGENi HBG000856.
    KOi K00036.

    Enzyme and pathway databases

    UniPathwayi UPA00115 ; UER00408 .

    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. "cDNA sequence of Chinese hamster glucose-6-phosphate Dehydrogenase."
      Perez M.L., Stamato T.D.
      Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovary.

    Entry informationi

    Entry nameiG6PD_CRIGR
    AccessioniPrimary (citable) accession number: O55044
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 91 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3