GCY1_YEAST
ID GCY1_YEAST Reviewed; 312 AA.
AC P14065; D6W2H9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Glycerol 2-dehydrogenase (NADP(+));
DE EC=1.1.1.156;
DE AltName: Full=Galactose-inducible crystallin-like protein 1;
GN Name=GCY1; Synonyms=GCY; OrderedLocusNames=YOR120W;
GN ORFNames=O31567, YOR3269W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24657 / D273-10B;
RX PubMed=2901985; DOI=10.1016/0014-5793(88)80240-0;
RA Oechsner U., Magdolen V., Bandlow W.;
RT "A nuclear yeast gene (GCY) encodes a polypeptide with high homology to a
RT vertebrate eye lens protein.";
RL FEBS Lett. 238:123-128(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25657;
RX PubMed=9395503; DOI=10.1074/jbc.272.50.31630;
RA Angermayr M., Bandlow W.;
RT "The type of basal promoter determines the regulated or constitutive mode
RT of transcription in the common control region of the yeast gene pair
RT GCY1/RIO1.";
RL J. Biol. Chem. 272:31630-31635(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP INDUCTION.
RX PubMed=2199324; DOI=10.1016/0378-1119(90)90445-w;
RA Magdolen V., Oechsner U., Trommler P., Bandlow W.;
RT "Transcriptional control by galactose of a yeast gene encoding a protein
RT homologous to mammalian aldo/keto reductases.";
RL Gene 90:105-114(1990).
RN [8]
RP INDUCTION.
RX PubMed=9038161; DOI=10.1074/jbc.272.9.5544;
RA Norbeck J., Blomberg A.;
RT "Metabolic and regulatory changes associated with growth of Saccharomyces
RT cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol
RT dissimilation via the dihydroxyacetone pathway.";
RL J. Biol. Chem. 272:5544-5554(1997).
RN [9]
RP INDUCTION.
RX PubMed=9435793; DOI=10.1007/s004380050616;
RA Angermayr M., Bandlow W.;
RT "The general regulatory factor Reb1p controls basal, but not Gal4p-
RT mediated, transcription of the GCY1 gene in yeast.";
RL Mol. Gen. Genet. 256:682-689(1997).
RN [10]
RP CRYSTALLIZATION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10818358; DOI=10.1107/s0907444900004704;
RA Hur E., Wilson D.K.;
RT "Crystallization and aldo-keto reductase activity of Gcy1p from
RT Saccharomyces cerevisiae.";
RL Acta Crystallogr. D 56:763-765(2000).
RN [11]
RP FUNCTION.
RX PubMed=11113971;
RX DOI=10.1002/1097-0061(200012)16:16<1483::aid-yea642>3.0.co;2-k;
RA Costenoble R., Valadi H., Gustafsson L., Niklasson C., Franzen C.J.;
RT "Microaerobic glycerol formation in Saccharomyces cerevisiae.";
RL Yeast 16:1483-1495(2000).
RN [12]
RP IDENTIFICATION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11306085; DOI=10.1016/s0009-2797(00)00258-1;
RA Petrash J.M., Murthy B.S., Young M., Morris K., Rikimaru L., Griest T.A.,
RA Harter T.;
RT "Functional genomic studies of aldo-keto reductases.";
RL Chem. Biol. Interact. 130:673-683(2001).
RN [13]
RP INDUCTION.
RX PubMed=12536147; DOI=10.1074/jbc.m210932200;
RA Angermayr M., Bandlow W.;
RT "Permanent nucleosome exclusion from the Gal4p-inducible yeast GCY1
RT promoter.";
RL J. Biol. Chem. 278:11026-11031(2003).
RN [14]
RP FUNCTION.
RX PubMed=15127164; DOI=10.1007/s00253-004-1624-4;
RA Izawa S., Sato M., Yokoigawa K., Inoue Y.;
RT "Intracellular glycerol influences resistance to freeze stress in
RT Saccharomyces cerevisiae: analysis of a quadruple mutant in glycerol
RT dehydrogenase genes and glycerol-enriched cells.";
RL Appl. Microbiol. Biotechnol. 66:108-114(2004).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF TYR-56.
RX PubMed=17140678; DOI=10.1016/j.bbamcr.2006.10.009;
RA Chang Q., Griest T.A., Harter T.M., Petrash J.M.;
RT "Functional studies of aldo-keto reductases in Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1773:321-329(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [17]
RP RNA-BINDING.
RX PubMed=20844764; DOI=10.1371/journal.pone.0012671;
RA Tsvetanova N.G., Klass D.M., Salzman J., Brown P.O.;
RT "Proteome-wide search reveals unexpected RNA-binding proteins in
RT Saccharomyces cerevisiae.";
RL PLoS ONE 5:E12671-E12671(2010).
RN [18]
RP FUNCTION.
RX PubMed=22979944; DOI=10.1111/jam.12013;
RA Jung J.Y., Kim T.Y., Ng C.Y., Oh M.K.;
RT "Characterization of GCY1 in Saccharomyces cerevisiae by metabolic
RT profiling.";
RL J. Appl. Microbiol. 113:1468-1478(2012).
RN [19]
RP INDUCTION.
RX PubMed=22842922; DOI=10.1038/ncb2549;
RA Tkach J.M., Yimit A., Lee A.Y., Riffle M., Costanzo M., Jaschob D.,
RA Hendry J.A., Ou J., Moffat J., Boone C., Davis T.N., Nislow C., Brown G.W.;
RT "Dissecting DNA damage response pathways by analysing protein localization
RT and abundance changes during DNA replication stress.";
RL Nat. Cell Biol. 14:966-976(2012).
RN [20]
RP FUNCTION.
RX PubMed=23896974; DOI=10.1007/s10295-013-1311-5;
RA Zhang L., Tang Y., Guo Z., Shi G.;
RT "Engineering of the glycerol decomposition pathway and cofactor regulation
RT in an industrial yeast improves ethanol production.";
RL J. Ind. Microbiol. Biotechnol. 40:1153-1160(2013).
RN [21]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF GLN-29; LYS-264; ASN-267 AND ARG-270.
RX PubMed=23770562; DOI=10.4014/jmb.1305.05030;
RA Yoon S.A., Kim H.K.;
RT "Development of a bioconversion system using Saccharomyces cerevisiae
RT reductase YOR120W and Bacillus subtilis glucose dehydrogenase for chiral
RT alcohol synthesis.";
RL J. Microbiol. Biotechnol. 23:1395-1402(2013).
CC -!- FUNCTION: Glycerol dehydrogenase involved in glycerol catabolism under
CC microaerobic conditions. Has mRNA binding activity.
CC {ECO:0000269|PubMed:11113971, ECO:0000269|PubMed:15127164,
CC ECO:0000269|PubMed:17140678, ECO:0000269|PubMed:22979944,
CC ECO:0000269|PubMed:23770562, ECO:0000269|PubMed:23896974}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol + NADP(+) = dihydroxyacetone + H(+) + NADPH;
CC Xref=Rhea:RHEA:12753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.156; Evidence={ECO:0000269|PubMed:10818358,
CC ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678,
CC ECO:0000269|PubMed:23770562};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.3 mM for D,L-glyceraldehyde {ECO:0000269|PubMed:10818358,
CC ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678,
CC ECO:0000269|PubMed:23770562};
CC KM=0.007 mM for NADPH {ECO:0000269|PubMed:10818358,
CC ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678,
CC ECO:0000269|PubMed:23770562};
CC KM=0.13 mM for p-nitrobenzaldehyde {ECO:0000269|PubMed:10818358,
CC ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678,
CC ECO:0000269|PubMed:23770562};
CC KM=5.2 mM for benzaldehyde {ECO:0000269|PubMed:10818358,
CC ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678,
CC ECO:0000269|PubMed:23770562};
CC KM=8.7 mM for phenylglyoxal {ECO:0000269|PubMed:10818358,
CC ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678,
CC ECO:0000269|PubMed:23770562};
CC KM=50 mM for acrolein {ECO:0000269|PubMed:10818358,
CC ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678,
CC ECO:0000269|PubMed:23770562};
CC KM=54 mM for butyraldehyde {ECO:0000269|PubMed:10818358,
CC ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678,
CC ECO:0000269|PubMed:23770562};
CC KM=0.724 mM for ethyl-4-chloro-3-oxo-butanoate
CC {ECO:0000269|PubMed:10818358, ECO:0000269|PubMed:11306085,
CC ECO:0000269|PubMed:17140678, ECO:0000269|PubMed:23770562};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:10818358,
CC ECO:0000269|PubMed:11306085, ECO:0000269|PubMed:17140678,
CC ECO:0000269|PubMed:23770562};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Expression is under the control of GAL4 and REB1, and is
CC both positively controlled by galactose and negatively by glucose. Also
CC induced by salt stress and in response to DNA replication stress.
CC {ECO:0000269|PubMed:12536147, ECO:0000269|PubMed:2199324,
CC ECO:0000269|PubMed:22842922, ECO:0000269|PubMed:9038161,
CC ECO:0000269|PubMed:9435793}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X13228; CAA31615.1; -; Genomic_DNA.
DR EMBL; X96740; CAA65512.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62107.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64040.1; -; Genomic_DNA.
DR EMBL; Z75028; CAA99318.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10895.1; -; Genomic_DNA.
DR PIR; S22846; S22846.
DR RefSeq; NP_014763.1; NM_001183539.1.
DR AlphaFoldDB; P14065; -.
DR SMR; P14065; -.
DR BioGRID; 34516; 51.
DR DIP; DIP-6342N; -.
DR IntAct; P14065; 2.
DR MINT; P14065; -.
DR STRING; 4932.YOR120W; -.
DR iPTMnet; P14065; -.
DR MaxQB; P14065; -.
DR PaxDb; P14065; -.
DR PRIDE; P14065; -.
DR TopDownProteomics; P14065; -.
DR EnsemblFungi; YOR120W_mRNA; YOR120W; YOR120W.
DR GeneID; 854287; -.
DR KEGG; sce:YOR120W; -.
DR SGD; S000005646; GCY1.
DR VEuPathDB; FungiDB:YOR120W; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000176580; -.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; P14065; -.
DR OMA; YSSECAL; -.
DR BioCyc; YEAST:YOR120W-MON; -.
DR PRO; PR:P14065; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P14065; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:SGD.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IDA:SGD.
DR GO; GO:0047953; F:glycerol 2-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:1990042; F:glycerol dehydrogenase [NAD(P)+] activity; IMP:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:SGD.
DR GO; GO:0019568; P:arabinose catabolic process; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
DR GO; GO:0042843; P:D-xylose catabolic process; IDA:SGD.
DR GO; GO:0061610; P:glycerol to glycerone phosphate metabolic process; IMP:SGD.
DR CDD; cd19117; AKR_AKR3A1-2; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044489; AKR3A.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycerol metabolism; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..312
FT /note="Glycerol 2-dehydrogenase (NADP(+))"
FT /id="PRO_0000124611"
FT ACT_SITE 56
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220..274
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 81
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 29
FT /note="Q->K: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:23770562"
FT MUTAGEN 56
FT /note="Y->L: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:17140678"
FT MUTAGEN 264
FT /note="K->R: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:23770562"
FT MUTAGEN 267
FT /note="N->Q: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:23770562"
FT MUTAGEN 270
FT /note="R->H,Y,K: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:23770562"
SQ SEQUENCE 312 AA; 35079 MW; 77B9D31C228334A4 CRC64;
MPATLHDSTK ILSLNTGAQI PQIGLGTWQS KENDAYKAVL TALKDGYRHI DTAAIYRNED
QVGQAIKDSG VPREEIFVTT KLWCTQHHEP EVALDQSLKR LGLDYVDLYL MHWPARLDPA
YIKNEDILSV PTKKDGSRAV DITNWNFIKT WELMQELPKT GKTKAVGVSN FSINNLKDLL
ASQGNKLTPA ANQVEIHPLL PQDELINFCK SKGIVVEAYS PLGSTDAPLL KEPVILEIAK
KNNVQPGHVV ISWHVQRGYV VLPKSVNPDR IKTNRKIFTL STEDFEAINN ISKEKGEKRV
VHPNWSPFEV FK
