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Database: UniProt
Entry: P53100
LinkDB: P53100
Original site: P53100 
ID   YGT5_YEAST              Reviewed;         379 AA.
AC   P53100; D6VTW9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   13-FEB-2019, entry version 142.
DE   RecName: Full=Putative 2-hydroxyacid dehydrogenase YGL185C;
DE            EC=1.-.-.-;
GN   OrderedLocusNames=YGL185C; ORFNames=G1380;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9046087;
RX   DOI=10.1002/(SICI)1097-0061(199701)13:1<55::AID-YEA48>3.3.CO;2-0;
RA   Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P.,
RA   Bruschi C.V.;
RT   "Sequencing of a 40.5 kb fragment located on the left arm of
RT   chromosome VII from Saccharomyces cerevisiae.";
RL   Yeast 13:55-64(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
RA   Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
RA   Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
RA   Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
RA   Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
RA   Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
RA   Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
RA   Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
RA   Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
RA   Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
RA   Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
RA   Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
RA   Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
RA   Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
RA   Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
RA   Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
RA   Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
RA   Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
RA   Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
RA   van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
RA   Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
RA   Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
RA   Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
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   [4]
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).
CC   -!- MISCELLANEOUS: Present with 1430 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; X91489; CAA62789.1; -; Genomic_DNA.
DR   EMBL; Z72707; CAA96897.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07930.1; -; Genomic_DNA.
DR   PIR; S61132; S61132.
DR   RefSeq; NP_011330.1; NM_001181050.1.
DR   ProteinModelPortal; P53100; -.
DR   BioGrid; 33070; 77.
DR   DIP; DIP-2562N; -.
DR   IntAct; P53100; 3.
DR   MINT; P53100; -.
DR   STRING; 4932.YGL185C; -.
DR   MaxQB; P53100; -.
DR   PaxDb; P53100; -.
DR   PRIDE; P53100; -.
DR   EnsemblFungi; YGL185C_mRNA; YGL185C_mRNA; YGL185C.
DR   GeneID; 852690; -.
DR   KEGG; sce:YGL185C; -.
DR   EuPathDB; FungiDB:YGL185C; -.
DR   SGD; S000003153; YGL185C.
DR   GeneTree; ENSGT00940000176460; -.
DR   HOGENOM; HOG000246508; -.
DR   InParanoid; P53100; -.
DR   OMA; CIVLCSR; -.
DR   BioCyc; YEAST:G3O-30670-MONOMER; -.
DR   PRO; PR:P53100; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IMP:SGD.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; ISS:SGD.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    379       Putative 2-hydroxyacid dehydrogenase
FT                                YGL185C.
FT                                /FTId=PRO_0000076037.
FT   NP_BIND     207    208       NAD. {ECO:0000250}.
FT   NP_BIND     291    293       NAD. {ECO:0000250}.
FT   NP_BIND     341    344       NAD. {ECO:0000250}.
FT   ACT_SITE    293    293       {ECO:0000250}.
FT   ACT_SITE    322    322       {ECO:0000250}.
FT   ACT_SITE    341    341       Proton donor. {ECO:0000250}.
FT   BINDING     317    317       NAD. {ECO:0000250}.
SQ   SEQUENCE   379 AA;  42984 MW;  5DEAAE194CA6BA96 CRC64;
     MCDSPATTGK PTILFIADPC ETSATLNSKA FKEKFRILRY QLDTKEAFLN FLERHEQDKI
     CAIYAGFPAF KKIGGMTRSI IEHKSFPRKN LKCIVLCSRG YDGWDLDTLR KHEIRLYNYQ
     DDENEKLIDD LKLHQVGNDV ADCALWHILE GFRKFSYYQK LSRETGNTLT ARAKAAEKSG
     FAFGHELGNM FAESPRGKKC LILGLGSIGK QVAYKLQYGL GMEIHYCKRS EDCTMSQNES
     WKFHLLDETI YAKLYQFHAI VVTLPGTPQT EHLINRKFLE HCNPGLILVN LGRGKILDLR
     AVSDALVTGR INHLGLDVFN KEPEIDEKIR SSDRLTSITP HLGSATKDVF EQSCELALTR
     ILRVVSGEAA SDEHFSRVV
//
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