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P11410

- G6PD_CYBJA

UniProt

P11410 - G6PD_CYBJA

Protein

Glucose-6-phosphate 1-dehydrogenase

Gene
N/A
Organism
Cyberlindnera jadinii (Torula yeast) (Pichia jadinii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (01 Apr 1993)
      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 sitei49 – 491NADPBy similarity
    Binding sitei149 – 1491NADP; via carbonyl oxygenBy similarity
    Binding sitei149 – 1491SubstrateBy similarity
    Binding sitei217 – 2171SubstrateBy similarity
    Binding sitei236 – 2361SubstrateBy similarity
    Active sitei241 – 2411Proton acceptorBy similarity
    Binding sitei335 – 3351SubstrateBy similarity
    Binding sitei369 – 3691SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 228NADPBy similarity

    GO - Molecular functioni

    1. glucose-6-phosphate dehydrogenase activity Source: UniProtKB-EC
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. 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
    OrganismiCyberlindnera jadinii (Torula yeast) (Pichia jadinii)
    Taxonomic identifieri4903 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeCyberlindnera

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 495495Glucose-6-phosphate 1-dehydrogenasePRO_0000068105Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylserine

    Keywords - PTMi

    Acetylation

    Structurei

    3D structure databases

    ProteinModelPortaliP11410.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni179 – 1835Substrate bindingBy similarity

    Sequence similaritiesi

    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.

    P11410-1 [UniParc]FASTAAdd to Basket

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    SYDSFGDRVT IIVFGASGDL ARKKTFPALF GLFREKQLPS TVQIIGYARS    50
    HLSDKDFKDY ISSHFKGGDD KTKEDFLNLC SYISDPYDTD EGYKKLEARC 100
    QEYESKHNVK VPERLFYLAL PPSVFHTVCE QVKKNVYPKN EKSRIIIEKP 150
    FGRDLETYRE LQKQISPLFT EDEVYRIDHY LGKEMVKNLL VLRFGNELFS 200
    GIWNNKHITS VQISFKEAFG TEGRGGYFDN IGIIRDVMQN HLLQVLTLLT 250
    MERPVSFDPE AVRDEKVKVL KAFDKIDVND VLLGQYGKSE DGTKPGYLDD 300
    STVKPNSKAV TYAAFRVNIH NERWDGVPIV LRAGKALDEG KAEIRIQFKP 350
    VAKGMFKEIQ RNELVIRIQP NEAIYLKINS KIPGISTETS LTDLDLTYST 400
    RYSKDFWIPE AYEALIRDCY LGNHSNFVRD DELEVSWKLF TPLLEAVEKE 450
    ENVKLESYPY GSKGPKELRK YLIDHGYVFN DPGTYQWPLT NTDVK 495
    Length:495
    Mass (Da):57,029
    Last modified:April 1, 1993 - v2
    Checksum:iB6944216F4B4C8D8
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071H → G.
    Natural varianti138 – 1381P → M.
    Natural varianti416 – 4161I → T.

    Sequence databases

    PIRiS11078.
    S29381.

    Cross-referencesi

    Sequence databases

    PIRi S11078.
    S29381.

    3D structure databases

    ProteinModelPortali P11410.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Glucose-6-phosphate dehydrogenase. Structure-function relationships and the Pichia jadinii enzyme structure."
      Jeffery J., Persson B., Wood I., Bergman T., Jeffery R., Joernvall H.
      Eur. J. Biochem. 212:41-49(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "Glucose-6-phosphate dehydrogenase. Characterization of a reactive lysine residue in the Pichia jadinii enzyme reveals a limited structural variation in a functionally significant segment."
      Jeffery J., Wood I., McLeod A., Jeffery R., Joernvall H.
      Biochem. Biophys. Res. Commun. 160:1290-1295(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 177-187.
      Strain: ATCC 9950 / CBS 5609 / DSM 2361 / NBRC 0998 / NRRL Y-900.
    3. "Alcoholytic deblocking of N-terminally acetylated peptides and proteins for sequence analysis."
      Bergman T., Gheorghe M.T., Hjelmqvist L., Joernvall H.
      FEBS Lett. 390:199-202(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10.

    Entry informationi

    Entry nameiG6PD_CYBJA
    AccessioniPrimary (citable) accession number: P11410
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

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

    External Data

    Dasty 3