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Protein

Glycerol 2-dehydrogenase (NADP(+))

Gene

GCY1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. Has mRNA binding activity.6 Publications

Catalytic activityi

Glycerol + NADP+ = glycerone + NADPH.4 Publications

Kineticsi

  1. KM=11.3 mM for D,L-glyceraldehyde4 Publications
  2. KM=0.007 mM for NADPH4 Publications
  3. KM=0.13 mM for p-nitrobenzaldehyde4 Publications
  4. KM=5.2 mM for benzaldehyde4 Publications
  5. KM=8.7 mM for phenylglyoxal4 Publications
  6. KM=50 mM for acrolein4 Publications
  7. KM=54 mM for butyraldehyde4 Publications
  8. KM=0.724 mM for ethyl-4-chloro-3-oxo-butanoate4 Publications

    pH dependencei

    Optimum pH is 6.5.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei56 – 561Proton donorBy similarity
    Sitei81 – 811Lowers pKa of active site TyrBy similarity
    Binding sitei112 – 1121SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi220 – 27455NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    • alditol:NADP+ 1-oxidoreductase activity Source: SGD
    • aldo-keto reductase (NADP) activity Source: SGD
    • glycerol 2-dehydrogenase (NADP+) activity Source: UniProtKB-EC
    • glycerol dehydrogenase [NAD(P)+] activity Source: SGD
    • mRNA binding Source: SGD
    • oxidoreductase activity Source: SGD

    GO - Biological processi

    • arabinose catabolic process Source: SGD
    • cellular response to oxidative stress Source: SGD
    • D-xylose catabolic process Source: SGD
    • glycerol metabolic process Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycerol metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciYEAST:YOR120W-MONOMER.
    ReactomeiR-SCE-156590. Glutathione conjugation.
    R-SCE-193144. Estrogen biosynthesis.
    R-SCE-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    R-SCE-193775. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    R-SCE-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    R-SCE-196108. Pregnenolone biosynthesis.
    R-SCE-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    R-SCE-5365859. RA biosynthesis pathway.
    R-SCE-5652227. Fructose biosynthesis.
    R-SCE-5661270. Catabolism of glucuronate to xylulose-5-phosphate.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycerol 2-dehydrogenase (NADP(+)) (EC:1.1.1.156)
    Alternative name(s):
    Galactose-inducible crystallin-like protein 1
    Gene namesi
    Name:GCY1
    Synonyms:GCY
    Ordered Locus Names:YOR120W
    ORF Names:O31567, YOR3269W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XV

    Organism-specific databases

    EuPathDBiFungiDB:YOR120W.
    SGDiS000005646. GCY1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291Q → K: Decreases catalytic activity. 1 Publication
    Mutagenesisi56 – 561Y → L: Loss of catalytic activity. 1 Publication
    Mutagenesisi264 – 2641K → R: Decreases catalytic activity. 1 Publication
    Mutagenesisi267 – 2671N → Q: Decreases catalytic activity. 1 Publication
    Mutagenesisi270 – 2701R → H, Y or K: Decreases catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 312312Glycerol 2-dehydrogenase (NADP(+))PRO_0000124611Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei306 – 3061PhosphoserineCombined sources

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP14065.
    PeptideAtlasiP14065.
    TopDownProteomicsiP14065.

    PTM databases

    iPTMnetiP14065.

    Expressioni

    Inductioni

    Expression is under the control of GAL4 and REB1, and is both positively controlled by galactose and negatively by glucose. Also induced by salt stress and in response to DNA replication stress.5 Publications

    Interactioni

    Protein-protein interaction databases

    BioGridi34516. 27 interactions.
    DIPiDIP-6342N.
    IntActiP14065. 1 interaction.
    MINTiMINT-2493441.

    Structurei

    3D structure databases

    ProteinModelPortaliP14065.
    SMRiP14065. Positions 8-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    InParanoidiP14065.
    KOiK18097.
    OrthoDBiEOG7WQ83S.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 2 hits.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14065-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPATLHDSTK ILSLNTGAQI PQIGLGTWQS KENDAYKAVL TALKDGYRHI
    60 70 80 90 100
    DTAAIYRNED QVGQAIKDSG VPREEIFVTT KLWCTQHHEP EVALDQSLKR
    110 120 130 140 150
    LGLDYVDLYL MHWPARLDPA YIKNEDILSV PTKKDGSRAV DITNWNFIKT
    160 170 180 190 200
    WELMQELPKT GKTKAVGVSN FSINNLKDLL ASQGNKLTPA ANQVEIHPLL
    210 220 230 240 250
    PQDELINFCK SKGIVVEAYS PLGSTDAPLL KEPVILEIAK KNNVQPGHVV
    260 270 280 290 300
    ISWHVQRGYV VLPKSVNPDR IKTNRKIFTL STEDFEAINN ISKEKGEKRV
    310
    VHPNWSPFEV FK
    Length:312
    Mass (Da):35,079
    Last modified:January 1, 1990 - v1
    Checksum:i77B9D31C228334A4
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X13228 Genomic DNA. Translation: CAA31615.1.
    X96740 Genomic DNA. Translation: CAA65512.1.
    X90518 Genomic DNA. Translation: CAA62107.1.
    X94335 Genomic DNA. Translation: CAA64040.1.
    Z75028 Genomic DNA. Translation: CAA99318.1.
    BK006948 Genomic DNA. Translation: DAA10895.1.
    PIRiS22846.
    RefSeqiNP_014763.1. NM_001183539.1.

    Genome annotation databases

    EnsemblFungiiYOR120W; YOR120W; YOR120W.
    GeneIDi854287.
    KEGGisce:YOR120W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X13228 Genomic DNA. Translation: CAA31615.1.
    X96740 Genomic DNA. Translation: CAA65512.1.
    X90518 Genomic DNA. Translation: CAA62107.1.
    X94335 Genomic DNA. Translation: CAA64040.1.
    Z75028 Genomic DNA. Translation: CAA99318.1.
    BK006948 Genomic DNA. Translation: DAA10895.1.
    PIRiS22846.
    RefSeqiNP_014763.1. NM_001183539.1.

    3D structure databases

    ProteinModelPortaliP14065.
    SMRiP14065. Positions 8-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi34516. 27 interactions.
    DIPiDIP-6342N.
    IntActiP14065. 1 interaction.
    MINTiMINT-2493441.

    PTM databases

    iPTMnetiP14065.

    Proteomic databases

    MaxQBiP14065.
    PeptideAtlasiP14065.
    TopDownProteomicsiP14065.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYOR120W; YOR120W; YOR120W.
    GeneIDi854287.
    KEGGisce:YOR120W.

    Organism-specific databases

    EuPathDBiFungiDB:YOR120W.
    SGDiS000005646. GCY1.

    Phylogenomic databases

    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    InParanoidiP14065.
    KOiK18097.
    OrthoDBiEOG7WQ83S.

    Enzyme and pathway databases

    BioCyciYEAST:YOR120W-MONOMER.
    ReactomeiR-SCE-156590. Glutathione conjugation.
    R-SCE-193144. Estrogen biosynthesis.
    R-SCE-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    R-SCE-193775. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    R-SCE-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    R-SCE-196108. Pregnenolone biosynthesis.
    R-SCE-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    R-SCE-5365859. RA biosynthesis pathway.
    R-SCE-5652227. Fructose biosynthesis.
    R-SCE-5661270. Catabolism of glucuronate to xylulose-5-phosphate.

    Miscellaneous databases

    PROiP14065.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 2 hits.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A nuclear yeast gene (GCY) encodes a polypeptide with high homology to a vertebrate eye lens protein."
      Oechsner U., Magdolen V., Bandlow W.
      FEBS Lett. 238:123-128(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 24657 / D273-10B.
    2. "The type of basal promoter determines the regulated or constitutive mode of transcription in the common control region of the yeast gene pair GCY1/RIO1."
      Angermayr M., Bandlow W.
      J. Biol. Chem. 272:31630-31635(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 25657.
    3. "Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames."
      Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.
      Yeast 12:281-288(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. "Transcriptional control by galactose of a yeast gene encoding a protein homologous to mammalian aldo/keto reductases."
      Magdolen V., Oechsner U., Trommler P., Bandlow W.
      Gene 90:105-114(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    8. "Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway."
      Norbeck J., Blomberg A.
      J. Biol. Chem. 272:5544-5554(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    9. "The general regulatory factor Reb1p controls basal, but not Gal4p-mediated, transcription of the GCY1 gene in yeast."
      Angermayr M., Bandlow W.
      Mol. Gen. Genet. 256:682-689(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "Crystallization and aldo-keto reductase activity of Gcy1p from Saccharomyces cerevisiae."
      Hur E., Wilson D.K.
      Acta Crystallogr. D 56:763-765(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Microaerobic glycerol formation in Saccharomyces cerevisiae."
      Costenoble R., Valadi H., Gustafsson L., Niklasson C., Franzen C.J.
      Yeast 16:1483-1495(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: IDENTIFICATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    13. "Permanent nucleosome exclusion from the Gal4p-inducible yeast GCY1 promoter."
      Angermayr M., Bandlow W.
      J. Biol. Chem. 278:11026-11031(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    14. "Intracellular glycerol influences resistance to freeze stress in Saccharomyces cerevisiae: analysis of a quadruple mutant in glycerol dehydrogenase genes and glycerol-enriched cells."
      Izawa S., Sato M., Yokoigawa K., Inoue Y.
      Appl. Microbiol. Biotechnol. 66:108-114(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Functional studies of aldo-keto reductases in Saccharomyces cerevisiae."
      Chang Q., Griest T.A., Harter T.M., Petrash J.M.
      Biochim. Biophys. Acta 1773:321-329(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-56.
    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-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Proteome-wide search reveals unexpected RNA-binding proteins in Saccharomyces cerevisiae."
      Tsvetanova N.G., Klass D.M., Salzman J., Brown P.O.
      PLoS ONE 5:E12671-E12671(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING.
    18. "Characterization of GCY1 in Saccharomyces cerevisiae by metabolic profiling."
      Jung J.Y., Kim T.Y., Ng C.Y., Oh M.K.
      J. Appl. Microbiol. 113:1468-1478(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress."
      Tkach J.M., Yimit A., Lee A.Y., Riffle M., Costanzo M., Jaschob D., Hendry J.A., Ou J., Moffat J., Boone C., Davis T.N., Nislow C., Brown G.W.
      Nat. Cell Biol. 14:966-976(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    20. "Engineering of the glycerol decomposition pathway and cofactor regulation in an industrial yeast improves ethanol production."
      Zhang L., Tang Y., Guo Z., Shi G.
      J. Ind. Microbiol. Biotechnol. 40:1153-1160(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Development of a bioconversion system using Saccharomyces cerevisiae reductase YOR120W and Bacillus subtilis glucose dehydrogenase for chiral alcohol synthesis."
      Yoon S.A., Kim H.K.
      J. Microbiol. Biotechnol. 23:1395-1402(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLN-29; LYS-264; ASN-267 AND ARG-270.

    Entry informationi

    Entry nameiGCY1_YEAST
    AccessioniPrimary (citable) accession number: P14065
    Secondary accession number(s): D6W2H9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: June 8, 2016
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.