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P90593

- GPDA_TRYBB

UniProt

P90593 - GPDA_TRYBB

Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomal

Gene

GPD

Organism
Trypanosoma brucei brucei
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei90 – 901NADBy similarity
    Binding sitei118 – 1181NAD; via amide nitrogenBy similarity
    Binding sitei118 – 1181SubstrateBy similarity
    Binding sitei150 – 1501NAD; via amide nitrogenBy similarity
    Active sitei203 – 2031Proton acceptorBy similarity
    Binding sitei267 – 2671NADBy similarity
    Binding sitei293 – 2931NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 206NADBy similarity

    GO - Molecular functioni

    1. glycerol-3-phosphate dehydrogenase [NAD+] activity Source: UniProtKB-EC
    2. NAD binding Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. glycerol-3-phosphate catabolic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomal (EC:1.1.1.8)
    Gene namesi
    Name:GPD
    OrganismiTrypanosoma brucei brucei
    Taxonomic identifieri5702 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

    Subcellular locationi

    GO - Cellular componenti

    1. glycerol-3-phosphate dehydrogenase complex Source: InterPro
    2. glycosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Glycosome, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 354354Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomalPRO_0000138083Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP90593.
    SMRiP90593. Positions 7-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni267 – 2682Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi352 – 3543Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPiMF_00394. NAD_Glyc3P_dehydrog.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR013328. DH_multihelical.
    IPR006168. G3P_DH_NAD-dep.
    IPR006109. G3P_DH_NAD-dep_C.
    IPR017751. G3P_DH_NAD-dep_euk.
    IPR011128. G3P_DH_NAD-dep_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11728. PTHR11728. 1 hit.
    PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
    PF01210. NAD_Gly3P_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
    PRINTSiPR00077. GPDHDRGNASE.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
    PROSITEiPS00957. NAD_G3PDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P90593-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVSGVTYLKR GAVFGSGAFG TALACVLAKK CESVSVWHMN ANEARVVNQK    50
    HENVYFLPGA PLPANLTFTA DAEECAKGAE IVLFVIPTQF LRGFLQKNSH 100
    ILRNHVVSRN VPVVMCSKGI ERSSLLFPAQ ILEEFLPNYP IGVIAGPSFA 150
    IEVAKGMLTN VCTAAADINM ARKIQRIMTT SDGSFRCWAT TDVIGCEIAS 200
    AMKNVLAIAS GALKGLGTEN NARAALISRG LLEIRDLTLA LGGTGEAVFG 250
    LPGLGDLLLT CSSELSRNFT VGMKLGQGIS LEEIKRTSKA VAEGVATAEP 300
    LERLAKKHNA DLPICHEVYN VLYANGCAKR SFKKLNSCKL ADEGLPALPR 350
    TSKM 354
    Length:354
    Mass (Da):37,783
    Last modified:May 1, 1997 - v1
    Checksum:i12CE19AEDA9E4EC9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89738 Genomic DNA. Translation: CAA61890.1.
    PIRiT48649.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89738 Genomic DNA. Translation: CAA61890.1 .
    PIRi T48649.

    3D structure databases

    ProteinModelPortali P90593.
    SMRi P90593. Positions 7-348.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPi MF_00394. NAD_Glyc3P_dehydrog.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. DH_multihelical.
    IPR006168. G3P_DH_NAD-dep.
    IPR006109. G3P_DH_NAD-dep_C.
    IPR017751. G3P_DH_NAD-dep_euk.
    IPR011128. G3P_DH_NAD-dep_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11728. PTHR11728. 1 hit.
    Pfami PF07479. NAD_Gly3P_dh_C. 1 hit.
    PF01210. NAD_Gly3P_dh_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000114. Glycerol-3-P_dh. 1 hit.
    PRINTSi PR00077. GPDHDRGNASE.
    SUPFAMi SSF48179. SSF48179. 1 hit.
    TIGRFAMsi TIGR03376. glycerol3P_DH. 1 hit.
    PROSITEi PS00957. NAD_G3PDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the NAD-linked glycerol-3-phosphate dehydrogenases of Trypanosoma brucei brucei and Leishmania mexicana mexicana and expression of the trypanosome enzyme in Escherichia coli."
      Kohl L., Drmota T., Thi C.-D., Callens M., van Beeumen J., Opperdoes F.R., Michels P.A.M.
      Mol. Biochem. Parasitol. 76:159-173(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 427.

    Entry informationi

    Entry nameiGPDA_TRYBB
    AccessioniPrimary (citable) accession number: P90593
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3