GOR1_YEAST
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 03-AUG-2022, entry version 173.
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;
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 + H(+) + NADH;
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 + H(+) + NADPH;
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 + H(+) + NADH;
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 + H(+) + NADPH;
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; 25.
DR IntAct; P53839; 5.
DR MINT; P53839; -.
DR STRING; 4932.YNL274C; -.
DR iPTMnet; P53839; -.
DR MaxQB; P53839; -.
DR PaxDb; P53839; -.
DR PRIDE; P53839; -.
DR EnsemblFungi; YNL274C_mRNA; YNL274C; YNL274C.
DR GeneID; 855447; -.
DR KEGG; sce:YNL274C; -.
DR SGD; S000005218; GOR1.
DR VEuPathDB; FungiDB:YNL274C; -.
DR eggNOG; KOG0069; Eukaryota.
DR GeneTree; ENSGT00940000162740; -.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; P53839; -.
DR OMA; VHHQTLG; -.
DR BioCyc; MetaCyc:G3O-33268-MON; -.
DR BioCyc; YEAST:G3O-33268-MON; -.
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:0008465; F:glycerate dehydrogenase activity; IEA:RHEA.
DR GO; GO:0047964; F:glyoxylate reductase (NAD+) activity; IMP:SGD.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009436; P:glyoxylate catabolic process; IMP:SGD.
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 Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 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
