YGT5_YEAST
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 03-AUG-2022, entry version 157.
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; Saccharomycetes;
OC 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>3.0.co;2-9;
RA Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.;
RT "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII
RT 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., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Dephoure N.,
RA 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 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; 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 AlphaFoldDB; P53100; -.
DR SMR; P53100; -.
DR BioGRID; 33070; 78.
DR DIP; DIP-2562N; -.
DR IntAct; P53100; 3.
DR MINT; P53100; -.
DR STRING; 4932.YGL185C; -.
DR iPTMnet; P53100; -.
DR MaxQB; P53100; -.
DR PaxDb; P53100; -.
DR PRIDE; P53100; -.
DR EnsemblFungi; YGL185C_mRNA; YGL185C; YGL185C.
DR GeneID; 852690; -.
DR KEGG; sce:YGL185C; -.
DR SGD; S000003153; YGL185C.
DR VEuPathDB; FungiDB:YGL185C; -.
DR eggNOG; KOG0069; Eukaryota.
DR GeneTree; ENSGT00940000176460; -.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; P53100; -.
DR OMA; MEIHYCK; -.
DR BioCyc; YEAST:G3O-30670-MON; -.
DR PRO; PR:P53100; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53100; protein.
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 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 NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..379
FT /note="Putative 2-hydroxyacid dehydrogenase YGL185C"
FT /id="PRO_0000076037"
FT ACT_SITE 293
FT /evidence="ECO:0000250"
FT ACT_SITE 322
FT /evidence="ECO:0000250"
FT ACT_SITE 341
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 207..208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 291..293
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 341..344
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="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
