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Q00055

- GPD1_YEAST

UniProt

Q00055 - GPD1_YEAST

Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)] 1

Gene

GPD1

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 150 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the production and accumulation of glycerol during hyperosmotic stress conditions. Glycerol acts as a osmoregulator that prevents loss of water and turgor of the cells.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei129 – 1291NADBy similarity
    Binding sitei152 – 1521NAD; via amide nitrogenBy similarity
    Binding sitei152 – 1521SubstrateBy similarity
    Binding sitei185 – 1851NAD; via amide nitrogenBy similarity
    Active sitei245 – 2451Proton acceptorBy similarity
    Binding sitei310 – 3101NADBy similarity
    Binding sitei339 – 3391NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi41 – 466NADBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. glycerol-3-phosphate catabolic process Source: InterPro
    3. intracellular accumulation of glycerol Source: SGD
    4. NADH oxidation Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:YDL022W-MONOMER.
    YEAST:YDL022W-MONOMER.
    BRENDAi1.1.1.8. 984.
    ReactomeiREACT_191569. Synthesis of PA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycerol-3-phosphate dehydrogenase [NAD(+)] 1 (EC:1.1.1.8)
    Gene namesi
    Name:GPD1
    Synonyms:DAR1, HOR1, OSG1
    Ordered Locus Names:YDL022W
    ORF Names:D2830
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    SGDiS000002180. GPD1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. glycerol-3-phosphate dehydrogenase complex Source: InterPro
    3. nucleus Source: SGD
    4. peroxisome Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 391390Glycerol-3-phosphate dehydrogenase [NAD(+)] 1PRO_0000138100Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei24 – 241Phosphoserine1 Publication
    Modified residuei27 – 271Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ00055.
    PaxDbiQ00055.
    PeptideAtlasiQ00055.

    Expressioni

    Inductioni

    By osmotic stress and by methylglyoxal in a HOG pathway-dependent manner.2 Publications

    Gene expression databases

    GenevestigatoriQ00055.

    Interactioni

    Protein-protein interaction databases

    BioGridi32033. 55 interactions.
    DIPiDIP-6393N.
    IntActiQ00055. 3 interactions.
    MINTiMINT-2788005.
    STRINGi4932.YDL022W.

    Structurei

    Secondary structure

    1
    391
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 406
    Helixi44 – 5916
    Turni61 – 633
    Beta strandi64 – 718
    Beta strandi76 – 794
    Helixi82 – 865
    Turni87 – 893
    Turni93 – 953
    Beta strandi103 – 1097
    Helixi111 – 1155
    Beta strandi119 – 1235
    Helixi127 – 1293
    Helixi130 – 1378
    Turni138 – 1403
    Beta strandi146 – 1494
    Beta strandi155 – 1573
    Beta strandi160 – 1623
    Helixi164 – 1729
    Beta strandi175 – 1806
    Helixi185 – 1895
    Beta strandi194 – 1996
    Beta strandi209 – 2124
    Helixi215 – 2228
    Beta strandi227 – 2337
    Helixi235 – 25723
    Helixi261 – 28323
    Helixi289 – 2946
    Turni296 – 2983
    Helixi299 – 3079
    Helixi310 – 32011
    Helixi325 – 3339
    Helixi340 – 35415
    Helixi361 – 37111
    Helixi379 – 3835

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4FGWX-ray2.45A/B1-391[»]
    ProteinModelPortaliQ00055.
    SMRiQ00055. Positions 33-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni310 – 3112Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0240.
    GeneTreeiENSGT00390000003114.
    HOGENOMiHOG000246855.
    KOiK00006.
    OMAiMMEKFPL.
    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]
    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.

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

    Q00055-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAAADRLNL TSGHLNAGRK RSSSSVSLKA AEKPFKVTVI GSGNWGTTIA    50
    KVVAENCKGY PEVFAPIVQM WVFEEEINGE KLTEIINTRH QNVKYLPGIT 100
    LPDNLVANPD LIDSVKDVDI IVFNIPHQFL PRICSQLKGH VDSHVRAISC 150
    LKGFEVGAKG VQLLSSYITE ELGIQCGALS GANIATEVAQ EHWSETTVAY 200
    HIPKDFRGEG KDVDHKVLKA LFHRPYFHVS VIEDVAGISI CGALKNVVAL 250
    GCGFVEGLGW GNNASAAIQR VGLGEIIRFG QMFFPESREE TYYQESAGVA 300
    DLITTCAGGR NVKVARLMAT SGKDAWECEK ELLNGQSAQG LITCKEVHEW 350
    LETCGSVEDF PLFEAVYQIV YNNYPMKNLP DMIEELDLHE D 391
    Length:391
    Mass (Da):42,869
    Last modified:January 23, 2007 - v4
    Checksum:iF5F1F7F111F707D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti103 – 1075DNLVA → TIWLL in AAA18631. (PubMed:1676389)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161N → D in strain: WFB. 1 Publication
    Natural varianti143 – 1431S → A in strain: WFB. 1 Publication
    Natural varianti164 – 1641L → P in strain: WFB. 1 Publication
    Natural varianti183 – 1831N → S in strain: WFB. 1 Publication
    Natural varianti225 – 2251P → S in strain: WFB. 1 Publication
    Natural varianti256 – 2561E → V in strain: WFB. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z24454 Genomic DNA. Translation: CAA80827.1.
    X76859 Genomic DNA. Translation: CAA54189.1.
    U04621 Genomic DNA. Translation: AAA64936.1.
    AY598965 Genomic DNA. Translation: AAT27375.1.
    AY598968 Genomic DNA. Translation: AAT27378.1.
    Z48432 Genomic DNA. Translation: CAA88337.1.
    Z74071 Genomic DNA. Translation: CAA98582.1.
    EF596737 Genomic DNA. Translation: ABQ58864.1.
    M38740 Genomic DNA. Translation: AAA18631.1.
    BK006938 Genomic DNA. Translation: DAA11828.1.
    PIRiS40059.
    RefSeqiNP_010262.1. NM_001180081.1.

    Genome annotation databases

    EnsemblFungiiYDL022W; YDL022W; YDL022W.
    GeneIDi851539.
    KEGGisce:YDL022W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z24454 Genomic DNA. Translation: CAA80827.1 .
    X76859 Genomic DNA. Translation: CAA54189.1 .
    U04621 Genomic DNA. Translation: AAA64936.1 .
    AY598965 Genomic DNA. Translation: AAT27375.1 .
    AY598968 Genomic DNA. Translation: AAT27378.1 .
    Z48432 Genomic DNA. Translation: CAA88337.1 .
    Z74071 Genomic DNA. Translation: CAA98582.1 .
    EF596737 Genomic DNA. Translation: ABQ58864.1 .
    M38740 Genomic DNA. Translation: AAA18631.1 .
    BK006938 Genomic DNA. Translation: DAA11828.1 .
    PIRi S40059.
    RefSeqi NP_010262.1. NM_001180081.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4FGW X-ray 2.45 A/B 1-391 [» ]
    ProteinModelPortali Q00055.
    SMRi Q00055. Positions 33-385.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32033. 55 interactions.
    DIPi DIP-6393N.
    IntActi Q00055. 3 interactions.
    MINTi MINT-2788005.
    STRINGi 4932.YDL022W.

    Proteomic databases

    MaxQBi Q00055.
    PaxDbi Q00055.
    PeptideAtlasi Q00055.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL022W ; YDL022W ; YDL022W .
    GeneIDi 851539.
    KEGGi sce:YDL022W.

    Organism-specific databases

    SGDi S000002180. GPD1.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci MetaCyc:YDL022W-MONOMER.
    YEAST:YDL022W-MONOMER.
    BRENDAi 1.1.1.8. 984.
    Reactomei REACT_191569. Synthesis of PA.

    Miscellaneous databases

    NextBioi 968943.

    Gene expression databases

    Genevestigatori Q00055.

    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 ]
    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. "A gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) complements an osmosensitive mutant of Saccharomyces cerevisiae."
      Larsson K., Ansell R., Eriksson P., Adler L.
      Mol. Microbiol. 10:1101-1111(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-49.
    2. "GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway."
      Albertyn J., Hohmann S., Thevelein J.M., Prior B.A.
      Mol. Cell. Biol. 14:4135-4144(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
    3. "Cloning, sequence, and disruption of the Saccharomyces diastaticus DAR1 gene encoding a glycerol-3-phosphate dehydrogenase."
      Wang H.T., Rahaim P., Robbins P., Yocum R.R.
      J. Bacteriol. 176:7091-7095(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Diastaticus / ATCC 62933 / NRC 5704 / J132b.
    4. "Research on the mechanism of osmotolerance and thermotolerance of yeast."
      Ma X., Guo Y., Zhang F., Yu H., Kuang J., Yao J., Li Z., He G.
      Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-16; ALA-143; PRO-164; SER-183; SER-225 AND VAL-256.
      Strain: FHS and WFB.
    5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. "The effects of co-expression of ScGPD1 and AtNHX1 on the salt tolerance of yeast."
      Fu C., Zheng D.
      Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    8. "Cloning and characterisation of the Saccharomyces cerevisiae glycerol-3-phosphate dehydrogenase (GUT2) promoter."
      Sleep D., Ogden J.E., Roberts N.A., Goodey A.R.
      Gene 101:89-96(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107.
    9. Bienvenut W.V., Peters C.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-19 AND 271-278, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
      Norbeck J., Blomberg A.
      FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 8-16; 95-108 AND 160-173.
      Strain: ATCC 38531 / Y41.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. "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.
    14. "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-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    15. "The HOG MAP kinase pathway is required for the induction of methylglyoxal-responsive genes and determines methylglyoxal resistance in Saccharomyces cerevisiae."
      Aguilera J., Rodriguez-Vargas S., Prieto J.A.
      Mol. Microbiol. 56:228-239(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    16. "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-24 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGPD1_YEAST
    AccessioniPrimary (citable) accession number: Q00055
    Secondary accession number(s): A5YWB0
    , D6VRW8, Q6J5J2, Q6J5J5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 150 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 807 molecules/cell in log phase SD medium.1 Publication

    Caution

    Was originally thought to be GUT2, the FAD-dependent glycerol-3-phosphate dehydrogenase.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3