GenomeNet

Database: UniProt
Entry: P53839
LinkDB: P53839
Original site: P53839 
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   13-FEB-2019, entry version 156.
DE   RecName: Full=Glyoxylate reductase 1;
DE            EC=1.1.1.26;
GN   Name=GOR1; OrderedLocusNames=YNL274C; ORFNames=N0631;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
RA   Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
RA   Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
RA   Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
RA   Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
RA   Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
RA   Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
RA   Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
RA   Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
RA   Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
RA   Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
RA   Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
RA   Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
RT   and its 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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding 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.,
RA   Dephoure N., 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.,
RA   Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
RA   Rehling P., 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.
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
RT   Saccharomyces cerevisiae.";
RL   Yeast 24:129-136(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND IDENTIFICATION
RP   BY 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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Reversibly reduces glyoxylate to glycolate.
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;
CC         EC=1.1.1.26;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion.
CC   -!- MISCELLANEOUS: Present with 3280 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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   ProteinModelPortal; P53839; -.
DR   SMR; P53839; -.
DR   BioGrid; 35566; 22.
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_mRNA; YNL274C.
DR   GeneID; 855447; -.
DR   KEGG; sce:YNL274C; -.
DR   EuPathDB; FungiDB:YNL274C; -.
DR   SGD; S000005218; GOR1.
DR   GeneTree; ENSGT00940000162740; -.
DR   InParanoid; P53839; -.
DR   KO; K00015; -.
DR   OMA; KWIAHNG; -.
DR   BioCyc; MetaCyc:G3O-33268-MONOMER; -.
DR   BioCyc; YEAST:G3O-33268-MONOMER; -.
DR   Reactome; R-SCE-389661; Glyoxylate metabolism and glycine degradation.
DR   PRO; PR:P53839; -.
DR   Proteomes; UP000002311; Chromosome XIV.
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:0030267; F:glyoxylate reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0047964; F:glyoxylate reductase activity; IMP:SGD.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; ISS:SGD.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
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   Complete proteome; Cytoplasm; Mitochondrion; NAD; Nucleus;
KW   Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN         1    350       Glyoxylate reductase 1.
FT                                /FTId=PRO_0000076040.
FT   NP_BIND     173    174       NAD. {ECO:0000250}.
FT   NP_BIND     252    254       NAD. {ECO:0000250}.
FT   NP_BIND     301    304       NAD. {ECO:0000250}.
FT   ACT_SITE    254    254       {ECO:0000250}.
FT   ACT_SITE    283    283       {ECO:0000250}.
FT   ACT_SITE    301    301       Proton donor. {ECO:0000250}.
FT   BINDING     278    278       NAD. {ECO:0000250}.
FT   MOD_RES      31     31       Phosphothreonine.
FT                                {ECO:0000244|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
//
DBGET integrated database retrieval system