ID   GOR1_YEAST              Reviewed;         350 AA.
AC   P53839; D6W0S0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 187.
DE   RecName: Full=Glyoxylate reductase 1 {ECO:0000303|PubMed:17173333};
DE            EC=1.1.1.26 {ECO:0000269|PubMed:17173333};
DE            EC=1.1.1.79 {ECO:0000269|PubMed:17173333};
DE            EC=1.1.1.81 {ECO:0000269|PubMed:17173333};
GN   Name=GOR1 {ECO:0000303|PubMed:17173333}; OrderedLocusNames=YNL274C;
GN   ORFNames=N0631;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17173333; DOI=10.1002/yea.1434;
RA   Rintala E., Pitkanen J.P., Vehkomaki M.L., Penttila M., Ruohonen L.;
RT   "The ORF YNL274c (GOR1) codes for glyoxylate reductase in Saccharomyces
RT   cerevisiae.";
RL   Yeast 24:129-136(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Glyoxylate reductase that reversibly reduces glyoxylate to
CC       glycolate, or alternatively hydroxypyruvate to D-glycerate, using
CC       either NADPH or NADH as a cosubstrate (PubMed:17173333). Does not act
CC       as a hydroxyisocaproate dehydrogenase even though it also has minor
CC       activity on alpha-ketoisocaproate (PubMed:17173333).
CC       {ECO:0000269|PubMed:17173333}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycolate + NAD(+) = glyoxylate + NADH + H(+);
CC         Xref=Rhea:RHEA:18229, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.26;
CC         Evidence={ECO:0000269|PubMed:17173333};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18231;
CC         Evidence={ECO:0000269|PubMed:17173333};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycolate + NADP(+) = glyoxylate + NADPH + H(+);
CC         Xref=Rhea:RHEA:10992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.79;
CC         Evidence={ECO:0000269|PubMed:17173333};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10994;
CC         Evidence={ECO:0000269|PubMed:17173333};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NAD(+) = 3-hydroxypyruvate + NADH + H(+);
CC         Xref=Rhea:RHEA:17905, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC         ChEBI:CHEBI:17180, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.81;
CC         Evidence={ECO:0000269|PubMed:17173333};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17907;
CC         Evidence={ECO:0000269|PubMed:17173333};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + NADPH + H(+);
CC         Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC         ChEBI:CHEBI:17180, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.81;
CC         Evidence={ECO:0000269|PubMed:17173333};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18659;
CC         Evidence={ECO:0000269|PubMed:17173333};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}. Mitochondrion
CC       {ECO:0000269|PubMed:14576278}.
CC   -!- DISRUPTION PHENOTYPE: Leads to higher biomass concentration after
CC       diauxic shift. {ECO:0000269|PubMed:17173333}.
CC   -!- MISCELLANEOUS: Present with 3280 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; Z71550; CAA96182.1; -; Genomic_DNA.
DR   EMBL; AY692660; AAT92679.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10286.1; -; Genomic_DNA.
DR   PIR; S63248; S63248.
DR   RefSeq; NP_014125.1; NM_001183112.1.
DR   AlphaFoldDB; P53839; -.
DR   SMR; P53839; -.
DR   BioGRID; 35566; 27.
DR   FunCoup; P53839; 618.
DR   IntAct; P53839; 5.
DR   MINT; P53839; -.
DR   STRING; 4932.YNL274C; -.
DR   iPTMnet; P53839; -.
DR   PaxDb; 4932-YNL274C; -.
DR   PeptideAtlas; P53839; -.
DR   EnsemblFungi; YNL274C_mRNA; YNL274C; YNL274C.
DR   GeneID; 855447; -.
DR   KEGG; sce:YNL274C; -.
DR   AGR; SGD:S000005218; -.
DR   SGD; S000005218; GOR1.
DR   VEuPathDB; FungiDB:YNL274C; -.
DR   eggNOG; KOG0069; Eukaryota.
DR   HOGENOM; CLU_019796_1_2_1; -.
DR   InParanoid; P53839; -.
DR   OMA; PHIAWAY; -.
DR   OrthoDB; 9991913at2759; -.
DR   BioCyc; MetaCyc:G3O-33268-MONOMER; -.
DR   BioCyc; YEAST:G3O-33268-MONOMER; -.
DR   BioGRID-ORCS; 855447; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P53839; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53839; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0047964; F:glyoxylate reductase (NADH) activity; IMP:SGD.
DR   GO; GO:0030267; F:glyoxylate reductase (NADPH) activity; EXP:UniProtKB.
DR   GO; GO:0008465; F:hydroxypyruvate reductase (NADH) activity; EXP:UniProtKB.
DR   GO; GO:0120509; F:hydroxypyruvate reductase (NADPH) activity; EXP:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0009436; P:glyoxylate catabolic process; IMP:SGD.
DR   CDD; cd12168; Mand_dh_like; 1.
DR   FunFam; 3.40.50.720:FF:000026; Glyoxylate/hydroxypyruvate reductase B; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR050223; D-isomer_2-hydroxyacid_DH.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR10996:SF257; GLYOXYLATE REDUCTASE 1; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Mitochondrion; NAD; Nucleus; Oxidoreductase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..350
FT                   /note="Glyoxylate reductase 1"
FT                   /id="PRO_0000076040"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT   ACT_SITE        301
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT   BINDING         173..174
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT   BINDING         252..254
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT   BINDING         278
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT   BINDING         301..304
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT   MOD_RES         31
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   350 AA;  38831 MW;  5E934D00E8A9BB13 CRC64;
     MSKKPIVLKL GKDAFGDQAW GELEKIADVI TIPESTTREQ FLREVKDPQN KLSQVQVITR
     TARSVKNTGR FDEELALALP SSVVAVCHTG AGYDQIDVEP FKKRHIQVAN VPDLVSNATA
     DTHVFLLLGA LRNFGIGNRR LIEGNWPEAG PACGSPFGYD PEGKTVGILG LGRIGRCILE
     RLKPFGFENF IYHNRHQLPS EEEHGCEYVG FEEFLKRSDI VSVNVPLNHN THHLINAETI
     EKMKDGVVIV NTARGAVIDE QAMTDALRSG KIRSAGLDVF EYEPKISKEL LSMSQVLGLP
     HMGTHSVETR KKMEELVVEN AKNVILTGKV LTIVPELQNE DWPNESKPLV
//