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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: -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)DescriptionActionsGraphical viewLength
    Active sitei56Proton donorBy similarity1
    Sitei81Lowers pKa of active site TyrBy similarity1
    Binding sitei112SubstrateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi220 – 274NADPBy similarityAdd BLAST55

    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

    Keywordsi

    Molecular functionOxidoreductase
    Biological processGlycerol metabolism
    LigandNADP

    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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi29Q → K: Decreases catalytic activity. 1 Publication1
    Mutagenesisi56Y → L: Loss of catalytic activity. 1 Publication1
    Mutagenesisi264K → R: Decreases catalytic activity. 1 Publication1
    Mutagenesisi267N → Q: Decreases catalytic activity. 1 Publication1
    Mutagenesisi270R → H, Y or K: Decreases catalytic activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001246111 – 312Glycerol 2-dehydrogenase (NADP(+))Add BLAST312

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei306PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP14065
    PaxDbiP14065
    PRIDEiP14065
    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, 50 interactors
    DIPiDIP-6342N
    IntActiP14065, 8 interactors
    MINTiP14065
    STRINGi4932.YOR120W

    Structurei

    3D structure databases

    ProteinModelPortaliP14065
    SMRiP14065
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00850000132445
    HOGENOMiHOG000250272
    InParanoidiP14065
    KOiK18097
    OMAiMAPSTHF
    OrthoDBiEOG092C324N

    Family and domain databases

    CDDicd06660 Aldo_ket_red, 1 hit
    Gene3Di3.20.20.100, 1 hit
    InterProiView protein in InterPro
    IPR018170 Aldo/ket_reductase_CS
    IPR020471 Aldo/keto_reductase
    IPR023210 NADP_OxRdtase_dom
    IPR036812 NADP_OxRdtase_dom_sf
    PANTHERiPTHR11732 PTHR11732, 1 hit
    PfamiView protein in Pfam
    PF00248 Aldo_ket_red, 1 hit
    PIRSFiPIRSF000097 AKR, 1 hit
    PRINTSiPR00069 ALDKETRDTASE
    SUPFAMiSSF51430 SSF51430, 1 hit
    PROSITEiView protein in PROSITE
    PS00798 ALDOKETO_REDUCTASE_1, 1 hit
    PS00062 ALDOKETO_REDUCTASE_2, 1 hit
    PS00063 ALDOKETO_REDUCTASE_3, 1 hit

    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

    Similar proteinsi

    Entry informationi

    Entry nameiGCY1_YEAST
    AccessioniPrimary (citable) accession number: P14065
    Secondary accession number(s): D6W2H9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: March 28, 2018
    This is version 164 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health