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YP113_YEAST
ID   YP113_YEAST             Reviewed;         396 AA.
AC   Q02961; D6W3Q4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Putative 2-hydroxyacid dehydrogenase YPL113C;
DE            EC=1.-.-.-;
GN   OrderedLocusNames=YPL113C;
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=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(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   INDUCTION.
RX   PubMed=12525494; DOI=10.1074/jbc.m211692200;
RA   Albers E., Laize V., Blomberg A., Hohmann S., Gustafsson L.;
RT   "Ser3p (Yer081wp) and Ser33p (Yil074cp) are phosphoglycerate dehydrogenases
RT   in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 278:10264-10272(2003).
CC   -!- FUNCTION: Putative 2-hydroxyacid dehydrogenase. {ECO:0000250}.
CC   -!- INDUCTION: Glucose-repressed. {ECO:0000269|PubMed:12525494}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; U43503; AAB68248.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11320.1; -; Genomic_DNA.
DR   PIR; S62008; S62008.
DR   RefSeq; NP_015212.1; NM_001183927.1.
DR   AlphaFoldDB; Q02961; -.
DR   SMR; Q02961; -.
DR   BioGRID; 36067; 67.
DR   DIP; DIP-6633N; -.
DR   IntAct; Q02961; 1.
DR   STRING; 4932.YPL113C; -.
DR   MaxQB; Q02961; -.
DR   PaxDb; Q02961; -.
DR   PRIDE; Q02961; -.
DR   EnsemblFungi; YPL113C_mRNA; YPL113C; YPL113C.
DR   GeneID; 855990; -.
DR   KEGG; sce:YPL113C; -.
DR   SGD; S000006034; YPL113C.
DR   VEuPathDB; FungiDB:YPL113C; -.
DR   eggNOG; KOG0069; Eukaryota.
DR   GeneTree; ENSGT00940000176460; -.
DR   HOGENOM; CLU_019796_1_2_1; -.
DR   InParanoid; Q02961; -.
DR   OMA; RGSCIDE; -.
DR   BioCyc; YEAST:G3O-34014-MON; -.
DR   Reactome; R-SCE-389661; Glyoxylate metabolism and glycine degradation.
DR   PRO; PR:Q02961; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q02961; protein.
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   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.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..396
FT                   /note="Putative 2-hydroxyacid dehydrogenase YPL113C"
FT                   /id="PRO_0000234369"
FT   ACT_SITE        313
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        342
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        361
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         227..228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         311..313
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         361..364
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   396 AA;  45014 MW;  C271E5E20FC8ABAF CRC64;
     MITSIDIADV TYSAKPRILV PYKTQWEVAS HLPEYRKLAE RVEFYKYEMS TKDDFVKFLE
     THRINGFWLT EEFFTVLGNP SSYIEFFPAS LKVILVPWVG CDFIDGKLLR SKGITLCNIG
     PHAADHVTEL AIFLAISCFR MTSFWEYCFK YVENGNVEQC KKYISSDSYE IVTDSYHGQE
     MKFPSRTDKC KPNKDRKVVH LAEKYTVGGK KMESPMNKKV LILGFGSIGQ NIGSNLHKVF
     NMSIEYYKRT GPVQKSLLDY NAKYHSDLDD PNTWKNADLI ILALPSTAST NNIINRKSLA
     WCKDGVRIVN VGRGTCIDED VLLDALESGK VASCGLDVFK NEETRVKQEL LRRWDVTALP
     HIGSTVADMV IKQTLITLEN VQDIFVEGGD GKYVLN
 
 
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