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P90551

- GPDA_LEIME

UniProt

P90551 - GPDA_LEIME

Protein

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

Gene

GPD

Organism
Leishmania mexicana
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (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 sitei97 – 971NADBy similarity
    Binding sitei125 – 1251NAD; via amide nitrogen2 Publications
    Binding sitei125 – 1251Substrate1 Publication
    Binding sitei157 – 1571NAD; via amide nitrogen2 Publications
    Active sitei210 – 2101Proton acceptorCurated
    Binding sitei274 – 2741NADBy similarity
    Binding sitei298 – 2981NAD; via amide nitrogen2 Publications
    Binding sitei300 – 3001NAD2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi22 – 276NAD2 Publications

    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

    Enzyme and pathway databases

    SABIO-RKP90551.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomal (EC:1.1.1.8)
    Gene namesi
    Name:GPD
    OrganismiLeishmania mexicana
    Taxonomic identifieri5665 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

    Subcellular locationi

    Glycosome 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Glycosome, Peroxisome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi125 – 1251K → A or M: Loss of activity. 1 Publication
    Mutagenesisi210 – 2101K → A or M: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 366366Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomalPRO_0000262292Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Structurei

    Secondary structure

    1
    366
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 217
    Helixi25 – 3410
    Turni35 – 373
    Beta strandi38 – 447
    Helixi48 – 5710
    Turni61 – 633
    Beta strandi73 – 775
    Helixi79 – 835
    Beta strandi87 – 915
    Helixi95 – 10511
    Helixi107 – 11610
    Beta strandi120 – 1223
    Turni129 – 1313
    Helixi135 – 1395
    Turni140 – 1423
    Helixi145 – 1473
    Beta strandi148 – 1547
    Helixi157 – 1615
    Beta strandi166 – 1716
    Helixi175 – 18511
    Beta strandi190 – 1989
    Helixi200 – 22223
    Helixi227 – 24721
    Turni253 – 2564
    Turni258 – 2603
    Helixi261 – 2688
    Helixi274 – 28310
    Helixi288 – 2925
    Helixi300 – 31516
    Helixi320 – 33011
    Helixi335 – 3428
    Helixi343 – 3453

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EVYX-ray1.75A1-366[»]
    1EVZX-ray2.80A1-366[»]
    1JDJX-ray2.20A1-366[»]
    1M66X-ray1.90A1-366[»]
    1M67X-ray2.50A1-366[»]
    1N1EX-ray1.90A/B1-366[»]
    1N1GX-ray2.50A1-366[»]
    ProteinModelPortaliP90551.
    SMRiP90551. Positions 9-357.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP90551.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni274 – 2752Substrate binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi364 – 3663Microbody 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.
    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.
    PROSITEiPS00957. NAD_G3PDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P90551-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTKQHSAKD ELLYLNKAVV FGSGAFGTAL AMVLSKKCRE VCVWHMNEEE    50
    VRLVNEKREN VLFLKGVQLA SNITFTSDVE KAYNGAEIIL FVIPTQFLRG 100
    FFEKSGGNLI AYAKEKQVPV LVCTKGIERS TLKFPAEIIG EFLPSPLLSV 150
    LAGPSFAIEV ATGVFTCVSI ASADINVARR LQRIMSTGDR SFVCWATTDT 200
    VGCEVASAVK NVLAIGSGVA NGLGMGLNAR AALIMRGLLE IRDLTAALGG 250
    DGSAVFGLAG LGDLQLTCSS ELSRNFTVGK KLGKGLPIEE IQRTSKAVAE 300
    GVATADPLMR LAKQLKVKMP LCHQIYEIVY KKKNPRDALA DLLSCGLQDE 350
    GLPPLFKRSA STPSKL 366
    Length:366
    Mass (Da):39,272
    Last modified:May 1, 1997 - v1
    Checksum:iE47594525FC0CF44
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89739 Genomic DNA. Translation: CAA61891.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89739 Genomic DNA. Translation: CAA61891.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EVY X-ray 1.75 A 1-366 [» ]
    1EVZ X-ray 2.80 A 1-366 [» ]
    1JDJ X-ray 2.20 A 1-366 [» ]
    1M66 X-ray 1.90 A 1-366 [» ]
    1M67 X-ray 2.50 A 1-366 [» ]
    1N1E X-ray 1.90 A/B 1-366 [» ]
    1N1G X-ray 2.50 A 1-366 [» ]
    ProteinModelPortali P90551.
    SMRi P90551. Positions 9-357.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P90551.

    Miscellaneous databases

    EvolutionaryTracei P90551.

    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.
    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.
    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], SUBCELLULAR LOCATION.
    2. "A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana."
      Suresh S., Turley S., Opperdoes F.R., Michels P.A.M., Hol W.G.J.
      Structure 8:541-552(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.
    3. "Anomalous differences of light elements in determining precise binding modes of ligands to glycerol-3-phosphate dehydrogenase."
      Choe J., Suresh S., Wisedchaisri G., Kennedy K.J., Gelb M.H., Hol W.G.J.
      Chem. Biol. 9:1189-1197(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD ANALOG.
    4. "Leishmania mexicana glycerol-3-phosphate dehydrogenase showed conformational changes upon binding a bi-substrate adduct."
      Choe J., Guerra D., Michels P.A.M., Hol W.G.J.
      J. Mol. Biol. 329:335-349(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NAD, MUTAGENESIS OF LYS-125 AND LYS-210.

    Entry informationi

    Entry nameiGPDA_LEIME
    AccessioniPrimary (citable) accession number: P90551
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3