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P41911

- GPD2_YEAST

UniProt

P41911 - GPD2_YEAST

Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, mitochondrial

Gene

GPD2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the production of glycerol under anaerobic growth conditions. Glycerol production serves as a redox sink by consuming the excess cytosolic NADH during anaerobic metabolism.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei178 – 1781NADBy similarity
    Binding sitei201 – 2011NAD; via amide nitrogenBy similarity
    Binding sitei201 – 2011SubstrateBy similarity
    Binding sitei234 – 2341NAD; via amide nitrogenBy similarity
    Active sitei294 – 2941Proton acceptorBy similarity
    Binding sitei359 – 3591NADBy similarity
    Binding sitei388 – 3881NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi90 – 956NADBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycerol-3-phosphate catabolic process Source: InterPro
    2. glycerol metabolic process Source: SGD
    3. NADH oxidation Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciYEAST:YOL059W-MONOMER.
    ReactomeiREACT_191569. Synthesis of PA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, mitochondrial (EC:1.1.1.8)
    Gene namesi
    Name:GPD2
    Synonyms:GPD3
    Ordered Locus Names:YOL059W
    ORF Names:O1222
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOL059w.
    SGDiS000005420. GPD2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. glycerol-3-phosphate dehydrogenase complex Source: InterPro
    3. mitochondrion Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1616MitochondrionSequence AnalysisAdd
    BLAST
    Chaini17 – 440424Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, mitochondrialPRO_0000043410Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701Phosphoserine1 Publication
    Modified residuei72 – 721Phosphoserine5 Publications
    Modified residuei75 – 751Phosphoserine5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP41911.
    PaxDbiP41911.
    PeptideAtlasiP41911.

    Expressioni

    Inductioni

    By anaerobic growth conditions and other conditions leading to accumulation of cytosolic NADH.2 Publications

    Gene expression databases

    GenevestigatoriP41911.

    Interactioni

    Protein-protein interaction databases

    BioGridi34342. 55 interactions.
    DIPiDIP-1348N.
    IntActiP41911. 5 interactions.
    MINTiMINT-411876.
    STRINGi4932.YOL059W.

    Structurei

    3D structure databases

    ProteinModelPortaliP41911.
    SMRiP41911. Positions 83-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni359 – 3602Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0240.
    GeneTreeiENSGT00390000003114.
    HOGENOMiHOG000246855.
    KOiK00006.
    OMAiQIVYNNV.
    OrthoDBiEOG7V76H7.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    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]
    PRINTSiPR00077. GPDHDRGNASE.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
    PROSITEiPS00957. NAD_G3PDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P41911-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLAVRRLTRY TFLKRTHPVL YTRRAYKILP SRSTFLRRSL LQTQLHSKMT    50
    AHTNIKQHKH CHEDHPIRRS DSAVSIVHLK RAPFKVTVIG SGNWGTTIAK 100
    VIAENTELHS HIFEPEVRMW VFDEKIGDEN LTDIINTRHQ NVKYLPNIDL 150
    PHNLVADPDL LHSIKGADIL VFNIPHQFLP NIVKQLQGHV APHVRAISCL 200
    KGFELGSKGV QLLSSYVTDE LGIQCGALSG ANLAPEVAKE HWSETTVAYQ 250
    LPKDYQGDGK DVDHKILKLL FHRPYFHVNV IDDVAGISIA GALKNVVALA 300
    CGFVEGMGWG NNASAAIQRL GLGEIIKFGR MFFPESKVET YYQESAGVAD 350
    LITTCSGGRN VKVATYMAKT GKSALEAEKE LLNGQSAQGI ITCREVHEWL 400
    QTCELTQEFP LFEAVYQIVY NNVRMEDLPE MIEELDIDDE 440
    Length:440
    Mass (Da):49,422
    Last modified:October 1, 1996 - v2
    Checksum:iFA6C07034D3EC720
    GO

    Sequence cautioni

    The sequence CAA84532.1 differs from that shown. Reason: Frameshift at position 411.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35169 Genomic DNA. Translation: CAA84532.1. Sequence problems.
    X91067 Genomic DNA. Translation: CAA62526.1.
    Z74801 Genomic DNA. Translation: CAA99068.1.
    AY558560 Genomic DNA. Translation: AAS56886.1.
    BK006948 Genomic DNA. Translation: DAA10724.1.
    PIRiS61719.
    RefSeqiNP_014582.1. NM_001183314.1.

    Genome annotation databases

    EnsemblFungiiYOL059W; YOL059W; YOL059W.
    GeneIDi854095.
    KEGGisce:YOL059W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35169 Genomic DNA. Translation: CAA84532.1 . Sequence problems.
    X91067 Genomic DNA. Translation: CAA62526.1 .
    Z74801 Genomic DNA. Translation: CAA99068.1 .
    AY558560 Genomic DNA. Translation: AAS56886.1 .
    BK006948 Genomic DNA. Translation: DAA10724.1 .
    PIRi S61719.
    RefSeqi NP_014582.1. NM_001183314.1.

    3D structure databases

    ProteinModelPortali P41911.
    SMRi P41911. Positions 83-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34342. 55 interactions.
    DIPi DIP-1348N.
    IntActi P41911. 5 interactions.
    MINTi MINT-411876.
    STRINGi 4932.YOL059W.

    Proteomic databases

    MaxQBi P41911.
    PaxDbi P41911.
    PeptideAtlasi P41911.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOL059W ; YOL059W ; YOL059W .
    GeneIDi 854095.
    KEGGi sce:YOL059W.

    Organism-specific databases

    CYGDi YOL059w.
    SGDi S000005420. GPD2.

    Phylogenomic databases

    eggNOGi COG0240.
    GeneTreei ENSGT00390000003114.
    HOGENOMi HOG000246855.
    KOi K00006.
    OMAi QIVYNNV.
    OrthoDBi EOG7V76H7.

    Enzyme and pathway databases

    BioCyci YEAST:YOL059W-MONOMER.
    Reactomei REACT_191569. Synthesis of PA.

    Miscellaneous databases

    NextBioi 975758.

    Gene expression databases

    Genevestigatori P41911.

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    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 ]
    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 GPD2, a second gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) in Saccharomyces cerevisiae, and its comparison with GPD1."
      Eriksson P., Andre L., Ansell R., Blomberg A., Adler L.
      Mol. Microbiol. 17:95-107(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of a 26 kb region on the left arm of yeast chromosome XV."
      Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.
      Yeast 12:67-76(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 90843 / S288c / FY73.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Physiological response to anaerobicity of glycerol-3-phosphate dehydrogenase mutants of Saccharomyces cerevisiae."
      Bjoerkqvist S., Ansell R., Adler L., Liden G.
      Appl. Environ. Microbiol. 63:128-132(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation."
      Ansell R., Granath K., Hohmann S., Thevelein J.M., Adler L.
      EMBO J. 16:2179-2187(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    11. "Distinct intracellular localization of Gpd1p and Gpd2p, the two yeast isoforms of NAD+-dependent glycerol-3-phosphate dehydrogenase, explains their different contributions to redox-driven glycerol production."
      Valadi A., Granath K., Gustafsson L., Adler L.
      J. Biol. Chem. 279:39677-39685(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION.
    12. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    13. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    14. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-72 AND SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGPD2_YEAST
    AccessioniPrimary (citable) accession number: P41911
    Secondary accession number(s): D6W208, P50905
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 8966 molecules/cell in log phase SD medium.1 Publication

    Caution

    It is uncertain whether Met-1 or Met-49 is the initiator.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3