KAR_YEAST
ID KAR_YEAST Reviewed; 312 AA.
AC Q07551; D6VRM6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=NADPH-dependent alpha-keto amide reductase;
DE Short=AKR-E;
DE EC=1.2.1.-;
DE AltName: Full=YKAR;
GN OrderedLocusNames=YDL124W; ORFNames=D2240;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 PROTEIN SEQUENCE OF 265-276, BIOPHYSICOCHEMICAL PROPERTIES,
RP CHARACTERIZATION, AND SUBUNIT.
RX PubMed=15564669; DOI=10.1271/bbb.68.2306;
RA Ishihara K., Yamamoto H., Mitsuhashi K., Nishikawa K., Tsuboi S., Tsuji H.,
RA Nakajima N.;
RT "Purification and characterization of alpha-keto amide reductase from
RT Saccharomyces cerevisiae.";
RL Biosci. Biotechnol. Biochem. 68:2306-2312(2004).
RN [4]
RP FUNCTION.
RX PubMed=11306085; DOI=10.1016/s0009-2797(00)00258-1;
RA Petrash J.M., Murthy B.S., Young M., Morris K., Rikimaru L., Griest T.A.,
RA Harter T.;
RT "Functional genomic studies of aldo-keto reductases.";
RL Chem. Biol. Interact. 130:673-683(2001).
RN [5]
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=12627397; DOI=10.1002/yea.960;
RA Salusjaervi L., Poutanen M., Pitkaenen J.-P., Koivistoinen H.,
RA Aristidou A., Kalkkinen N., Ruohonen L., Penttilae M.;
RT "Proteome analysis of recombinant xylose-fermenting Saccharomyces
RT cerevisiae.";
RL Yeast 20:295-314(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, 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: Reduces aromatic alpha-keto amides, aliphatic and aromatic
CC alpha-keto esters, but not beta-keto esters.
CC {ECO:0000269|PubMed:11306085}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=146 uM for o-chlorobenzoylformamide {ECO:0000269|PubMed:15564669};
CC KM=156 uM for m-chlorobenzoylformamide {ECO:0000269|PubMed:15564669};
CC KM=231 uM for p-chlorobenzoylformamide {ECO:0000269|PubMed:15564669};
CC KM=103 uM for benzoylformamide {ECO:0000269|PubMed:15564669};
CC KM=254 uM for 3-methyl-2-oxobutanoate {ECO:0000269|PubMed:15564669};
CC pH dependence:
CC Stable from pH 6 to 9.5. {ECO:0000269|PubMed:15564669};
CC Temperature dependence:
CC Thermostable up to 40 degrees Celsius. {ECO:0000269|PubMed:15564669};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15564669}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Transiently induced shortly after the switch from aerobic to
CC anaerobic growth (at protein level). {ECO:0000269|PubMed:12627397}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 4030 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; Z74172; CAA98692.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11736.1; -; Genomic_DNA.
DR PIR; S67667; S67667.
DR RefSeq; NP_010159.1; NM_001180183.1.
DR AlphaFoldDB; Q07551; -.
DR SMR; Q07551; -.
DR BioGRID; 31939; 81.
DR DIP; DIP-6607N; -.
DR IntAct; Q07551; 2.
DR STRING; 4932.YDL124W; -.
DR iPTMnet; Q07551; -.
DR UCD-2DPAGE; Q07551; -.
DR MaxQB; Q07551; -.
DR PaxDb; Q07551; -.
DR PRIDE; Q07551; -.
DR TopDownProteomics; Q07551; -.
DR EnsemblFungi; YDL124W_mRNA; YDL124W; YDL124W.
DR GeneID; 851433; -.
DR KEGG; sce:YDL124W; -.
DR SGD; S000002282; YDL124W.
DR VEuPathDB; FungiDB:YDL124W; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000164916; -.
DR HOGENOM; CLU_023205_0_3_1; -.
DR InParanoid; Q07551; -.
DR OMA; WCIDQDI; -.
DR BioCyc; YEAST:G3O-29523-MON; -.
DR PRO; PR:Q07551; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07551; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:SGD.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IDA:SGD.
DR GO; GO:0051268; F:alpha-keto amide reductase activity; IDA:SGD.
DR GO; GO:0051269; F:alpha-keto ester reductase activity; IDA:SGD.
DR GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IEA:InterPro.
DR GO; GO:0043603; P:cellular amide metabolic process; IDA:SGD.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IDA:SGD.
DR GO; GO:0042180; P:cellular ketone metabolic process; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
DR CDD; cd19120; AKR_AKR3C2-3; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044494; AKR3C2/3.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; NADP; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..312
FT /note="NADPH-dependent alpha-keto amide reductase"
FT /id="PRO_0000262755"
FT ACT_SITE 64
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 208..268
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 89
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 312 AA; 35561 MW; 165ADCB5C1952AF0 CRC64;
MSFHQQFFTL NNGNKIPAIA IIGTGTRWYK NEETDATFSN SLVEQIVYAL KLPGIIHIDA
AEIYRTYPEV GKALSLTEKP RNAIFLTDKY SPQIKMSDSP ADGLDLALKK MGTDYVDLYL
LHSPFVSKEV NGLSLEEAWK DMEQLYKSGK AKNIGVSNFA VEDLQRILKV AEVKPQVNQI
EFSPFLQNQT PGIYKFCQEH DILVEAYSPL GPLQKKTAQD DSQPFFEYVK ELSEKYIKSE
AQIILRWVTK RGVLPVTTSS KPQRISDAQN LFSFDLTAEE VDKITELGLE HEPLRLYWNK
LYGKYNYAAQ KV
