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 11-DEC-2019, entry version 156. 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; 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=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., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome 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., 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 1-14, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP 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., 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND IDENTIFICATION BY RP 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 insights RT 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 specificity CC acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L- CC allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously CC decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, CC D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate CC and L-glycerate. {ECO:0000269|PubMed:12535615}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-allo-threonine + NADP(+) = aminoacetone + CO2 + NADPH; CC Xref=Rhea:RHEA:43524, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58320, ChEBI:CHEBI:58349, ChEBI:CHEBI:58585; CC EC=1.1.1.381; Evidence={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 Celsius) CC {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 from pH CC 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 -!- INTERACTION: CC P39009:DUN1; NbExp=2; IntAct=EBI-27486, EBI-6194; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus CC {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 3210 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC 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 SMR; Q05016; -. DR BioGrid; 35404; 97. DR DIP; DIP-1671N; -. DR IntAct; Q05016; 14. DR MINT; Q05016; -. DR STRING; 4932.YMR226C; -. DR iPTMnet; Q05016; -. DR MaxQB; Q05016; -. DR PaxDb; Q05016; -. DR PRIDE; Q05016; -. DR TopDownProteomics; Q05016; -. DR EnsemblFungi; YMR226C_mRNA; YMR226C; YMR226C. DR GeneID; 855266; -. DR KEGG; sce:YMR226C; -. DR EuPathDB; FungiDB:YMR226C; -. DR SGD; S000004839; YMR226C. DR InParanoid; Q05016; -. DR KO; K16066; -. DR OMA; WRWMWET; -. DR BioCyc; YEAST:G3O-32907-MONOMER; -. DR PRO; PR:Q05016; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; Q05016; protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. 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 InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. 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; Cytoplasm; Direct protein sequencing; NADP; Nucleus; KW Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1..267 FT /note="NADP-dependent 3-hydroxy acid dehydrogenase" FT /id="PRO_0000054873" FT NP_BIND 20..25 FT /note="NADP" FT /evidence="ECO:0000269|Ref.7" FT NP_BIND 48..49 FT /note="NADP" FT /evidence="ECO:0000269|Ref.7" FT NP_BIND 75..76 FT /note="NADP" FT /evidence="ECO:0000269|Ref.7" FT NP_BIND 198..205 FT /note="NADP" FT /evidence="ECO:0000269|Ref.7" FT ACT_SITE 168 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001" FT BINDING 102 FT /note="NADP; via carbonyl oxygen" FT /evidence="ECO:0000269|Ref.7" FT BINDING 155 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 168 FT /note="NADP" FT /evidence="ECO:0000269|Ref.7" FT BINDING 172 FT /note="NADP" FT /evidence="ECO:0000269|Ref.7" FT MOD_RES 260 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19779198" FT HELIX 5..11 FT /evidence="ECO:0000244|PDB:3RKU" FT STRAND 15..20 FT /evidence="ECO:0000244|PDB:3RKU" FT HELIX 24..36 FT /evidence="ECO:0000244|PDB:3RKU" FT TURN 37..39 FT /evidence="ECO:0000244|PDB:3RKU" FT STRAND 41..48 FT /evidence="ECO:0000244|PDB:3RKU" FT HELIX 50..63 FT /evidence="ECO:0000244|PDB:3RKU" FT STRAND 68..73 FT /evidence="ECO:0000244|PDB:3RKU" FT HELIX 79..81 FT /evidence="ECO:0000244|PDB:3RKU" FT HELIX 82..87 FT /evidence="ECO:0000244|PDB:3RKU" FT HELIX 91..93 FT /evidence="ECO:0000244|PDB:3RKU" FT STRAND 98..101 FT /evidence="ECO:0000244|PDB:3RKU" FT HELIX 117..127 FT /evidence="ECO:0000244|PDB:3RKU" FT HELIX 129..145 FT /evidence="ECO:0000244|PDB:3RKU" FT STRAND 149..153 FT /evidence="ECO:0000244|PDB:3RKU" FT HELIX 156..158 FT /evidence="ECO:0000244|PDB:3RKU" FT HELIX 166..185 FT /evidence="ECO:0000244|PDB:3RKU" FT TURN 186..188 FT /evidence="ECO:0000244|PDB:3RKU" FT STRAND 192..199 FT /evidence="ECO:0000244|PDB:3RKU" FT STRAND 201..204 FT /evidence="ECO:0000244|PDB:3RKU" FT HELIX 205..209 FT /evidence="ECO:0000244|PDB:3RKU" FT TURN 210..212 FT /evidence="ECO:0000244|PDB:3RKU" FT HELIX 214..221 FT /evidence="ECO:0000244|PDB:3RKU" FT HELIX 229..240 FT /evidence="ECO:0000244|PDB:3RKU" FT STRAND 246..255 FT /evidence="ECO:0000244|PDB:3RKU" FT STRAND 258..260 FT /evidence="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 //