ID YM71_YEAST Reviewed; 267 AA. AC Q05016; D6W051; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 126. DE RecName: Full=NADP-dependent 3-hydroxy acid dehydrogenase {ECO:0000303|PubMed:12535615}; DE AltName: Full=L-allo-threonine dehydrogenase {ECO:0000303|PubMed:12535615}; DE EC=1.1.1.381 {ECO:0000269|PubMed:12535615}; GN OrderedLocusNames=YMR226C {ECO:0000312|SGD:S000004839}; GN ORFNames=YM9959.08C; 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=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., RA Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., RA Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome RT XIII."; RL Nature 387:90-93(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 PROTEIN SEQUENCE OF 1-14, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT. RX PubMed=12535615; DOI=10.1016/S1570-9639(02)00533-2; RA Fujisawa H., Nagata S., Misono H.; RT "Characterization of short-chain dehydrogenase/reductase homologues of RT Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C)."; RL Biochim. Biophys. Acta 1645:89-94(2003). 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides RT insights into evolution."; RL Science 325:1682-1686(2009). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH NADP. RA Huether R., Pacheco C.M., Duax W.L.; RT "Substrate fingerprint and the structure of NADP(+)-dependent serine RT dehydrogenase from Saccharomyces cerevisiae complexed with NADP(+)."; RL Submitted (APR-2011) to the PDB data bank. CC -!- FUNCTION: NADP-dependent dehydrogenase with broad substrate CC specificity acting on 3-hydroxy acids. Catalyzes the NADP- CC dependent oxidation of L-allo-threonine to L-2-amino-3-keto- CC butyrate, which is spontaneously decarboxylated into aminoacetone. CC Also acts on D-threonine, L-serine, D-serine, D-3- CC hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L- CC glycerate. {ECO:0000269|PubMed:12535615}. CC -!- CATALYTIC ACTIVITY: L-allo-threonine + NADP(+) = aminoacetone + CC CO(2) + NADPH. {ECO:0000269|PubMed:12535615}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.5 mM for NADP(+) (at pH 9 and at 30 degrees Celsius) CC {ECO:0000269|PubMed:12535615}; CC KM=95 mM for L-serine (at pH 9 and at 30 degrees Celsius) CC {ECO:0000269|PubMed:12535615}; CC KM=71 mM for D-serine (at pH 9 and at 30 degrees Celsius) CC {ECO:0000269|PubMed:12535615}; CC KM=7 mM for D-threonine (at pH 9 and at 30 degrees Celsius) CC {ECO:0000269|PubMed:12535615}; CC KM=3 mM for L-allo-threonine (at pH 9 and at 30 degrees Celsius) CC {ECO:0000269|PubMed:12535615}; CC KM=36 mM for L-3-hydroxyisobutyrate (at pH 9 and at 30 degrees CC Celsius) {ECO:0000269|PubMed:12535615}; CC KM=57 mM for D-3-hydroxyisobutyrate (at pH 9 and at 30 degrees CC Celsius) {ECO:0000269|PubMed:12535615}; CC KM=95 mM for L-3-hydroxybutyrate (at pH 9 and at 30 degrees CC Celsius) {ECO:0000269|PubMed:12535615}; CC Note=The highest catalytic efficiency was observed with L-allo- CC threonine. {ECO:0000269|PubMed:12535615}; CC pH dependence: CC Optimum pH is about 8.5 for the oxidation of L-serine. Stable CC from pH 7.5 to 10.5. {ECO:0000269|PubMed:12535615}; CC Temperature dependence: CC Stable up to 40 degrees Celsius. {ECO:0000269|PubMed:12535615}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12535615}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC Nucleus {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 3210 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z49939; CAA90197.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10125.1; -; Genomic_DNA. DR PIR; S57593; S57593. DR RefSeq; NP_013953.1; NM_001182733.1. DR PDB; 3RKU; X-ray; 2.60 A; A/B/C/D=1-267. DR PDBsum; 3RKU; -. DR ProteinModelPortal; Q05016; -. DR SMR; Q05016; 1-267. DR BioGrid; 35404; 38. DR DIP; DIP-1671N; -. DR IntAct; Q05016; 4. DR MINT; MINT-409559; -. DR iPTMnet; Q05016; -. DR MaxQB; Q05016; -. DR PeptideAtlas; Q05016; -. DR PRIDE; Q05016; -. DR EnsemblFungi; YMR226C; YMR226C; YMR226C. DR GeneID; 855266; -. DR KEGG; sce:YMR226C; -. DR EuPathDB; FungiDB:YMR226C; -. DR SGD; S000004839; YMR226C. DR GeneTree; ENSGT00830000128309; -. DR InParanoid; Q05016; -. DR KO; K16066; -. DR OMA; MEMGSAI; -. DR OrthoDB; EOG70612F; -. DR BioCyc; YEAST:G3O-32907-MONOMER; -. DR NextBio; 978870; -. DR PRO; PR:Q05016; -. DR Proteomes; UP000002311; Chromosome XIII. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:SGD. DR GO; GO:0016491; F:oxidoreductase activity; IDA:SGD. DR GO; GO:0031132; F:serine 3-dehydrogenase activity; IDA:SGD. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; KW NADP; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1 267 NADP-dependent 3-hydroxy acid FT dehydrogenase. FT /FTId=PRO_0000054873. FT NP_BIND 20 25 NADP. {ECO:0000269|Ref.7}. FT NP_BIND 48 49 NADP. {ECO:0000269|Ref.7}. FT NP_BIND 75 76 NADP. {ECO:0000269|Ref.7}. FT NP_BIND 198 205 NADP. {ECO:0000269|Ref.7}. FT ACT_SITE 168 168 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10001}. FT BINDING 102 102 NADP; via carbonyl oxygen. FT {ECO:0000269|Ref.7}. FT BINDING 155 155 Substrate. {ECO:0000250}. FT BINDING 168 168 NADP. {ECO:0000269|Ref.7}. FT BINDING 172 172 NADP. {ECO:0000269|Ref.7}. FT MOD_RES 260 260 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT HELIX 5 11 {ECO:0000244|PDB:3RKU}. FT STRAND 15 20 {ECO:0000244|PDB:3RKU}. FT HELIX 24 36 {ECO:0000244|PDB:3RKU}. FT TURN 37 39 {ECO:0000244|PDB:3RKU}. FT STRAND 41 48 {ECO:0000244|PDB:3RKU}. FT HELIX 50 63 {ECO:0000244|PDB:3RKU}. FT STRAND 68 73 {ECO:0000244|PDB:3RKU}. FT HELIX 79 81 {ECO:0000244|PDB:3RKU}. FT HELIX 82 87 {ECO:0000244|PDB:3RKU}. FT HELIX 91 93 {ECO:0000244|PDB:3RKU}. FT STRAND 98 101 {ECO:0000244|PDB:3RKU}. FT HELIX 117 127 {ECO:0000244|PDB:3RKU}. FT HELIX 129 145 {ECO:0000244|PDB:3RKU}. FT STRAND 149 153 {ECO:0000244|PDB:3RKU}. FT HELIX 156 158 {ECO:0000244|PDB:3RKU}. FT HELIX 166 185 {ECO:0000244|PDB:3RKU}. FT TURN 186 188 {ECO:0000244|PDB:3RKU}. FT STRAND 192 199 {ECO:0000244|PDB:3RKU}. FT STRAND 201 204 {ECO:0000244|PDB:3RKU}. FT HELIX 205 209 {ECO:0000244|PDB:3RKU}. FT TURN 210 212 {ECO:0000244|PDB:3RKU}. FT HELIX 214 221 {ECO:0000244|PDB:3RKU}. FT HELIX 229 240 {ECO:0000244|PDB:3RKU}. FT STRAND 246 255 {ECO:0000244|PDB:3RKU}. FT STRAND 258 260 {ECO:0000244|PDB:3RKU}. SQ SEQUENCE 267 AA; 29158 MW; 77FCD713F724A9D7 CRC64; MSQGRKAAER LAKKTVLITG ASAGIGKATA LEYLEASNGD MKLILAARRL EKLEELKKTI DQEFPNAKVH VAQLDITQAE KIKPFIENLP QEFKDIDILV NNAGKALGSD RVGQIATEDI QDVFDTNVTA LINITQAVLP IFQAKNSGDI VNLGSIAGRD AYPTGSIYCA SKFAVGAFTD SLRKELINTK IRVILIAPGL VETEFSLVRY RGNEEQAKNV YKDTTPLMAD DVADLIVYAT SRKQNTVIAD TLIFPTNQAS PHHIFRG //