ID BDH1_YEAST Reviewed; 382 AA. AC P39714; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 25-NOV-2008, entry version 70. DE RecName: Full=(R,R)-butanediol dehydrogenase; DE EC=1.1.1.4; GN Name=BDH1; Synonyms=BDH; OrderedLocusNames=YAL060W; ORFNames=FUN49; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=95249563; PubMed=7731988; RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., RA Storms R.K.; RT "The nucleotide sequence of chromosome I from Saccharomyces RT cerevisiae."; RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995). RN [2] RP CHARACTERIZATION. RC STRAIN=ATCC 90845 / FY834; RX MEDLINE=20549593; PubMed=10938079; DOI=10.1074/jbc.M003035200; RA Gonzalez E., Fernandez M.R., Larroy C., Sola L., Pericas M.A., RA Pares X., Biosca J.A.; RT "Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the RT Saccharomyces cerevisiae YAL060W gene product. Disruption and RT induction of the gene."; RL J. Biol. Chem. 275:35876-35885(2000). RN [3] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; 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). CC -!- CATALYTIC ACTIVITY: (R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + CC NADH. CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity). CC -!- SUBUNIT: Homodimer. CC -!- INTERACTION: CC P40054:SER3; NbExp=1; IntAct=EBI-3501, EBI-16961; CC -!- MISCELLANEOUS: Present with 8730 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U12980; AAC04974.1; -; Genomic_DNA. DR PIR; S51962; S51962. DR RefSeq; NP_009341.1; -. DR HSSP; O96496; 1E3J. DR DIP; DIP:5356N; -. DR IntAct; P39714; -. DR PeptideAtlas; P39714; -. DR Ensembl; YAL060W; Saccharomyces cerevisiae. DR GeneID; 851239; -. DR GenomeReviews; U00091_GR; YAL060W. DR KEGG; sce:YAL060W; -. DR NMPDR; fig|4932.3.peg.15; -. DR CYGD; YAL060w; -. DR SGD; S000000056; BDH1. DR HOGENOM; P39714; -. DR BioCyc; MetaCyc:MON-14023; -. DR LinkHub; P39714; -. DR NextBio; 968165; -. DR GermOnline; YAL060W; Saccharomyces cerevisiae. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0000721; F:(R,R)-butanediol dehydrogenase activity; IEA:EC. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006066; P:cellular alcohol metabolic process; IMP:SGD. DR GO; GO:0055114; P:oxidation reduction; IEA:InterPro. DR InterPro; IPR013154; AlcDHase_GroES-like. DR InterPro; IPR002085; AlcDHase_SF_Zn. DR InterPro; IPR013149; AlcDHase_Zn-bd. DR InterPro; IPR002328; AlcDHase_Zn_CS. DR PANTHER; PTHR11695; ADH_Sf_Zn; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 1: Evidence at protein level; KW Complete proteome; Metal-binding; NAD; Oxidoreductase; Zinc. FT CHAIN 1 382 (R,R)-butanediol dehydrogenase. FT /FTId=PRO_0000160788. FT METAL 39 39 Zinc 1; catalytic (By similarity). FT METAL 73 73 Zinc 1; catalytic (By similarity). FT METAL 103 103 Zinc 2 (By similarity). FT METAL 120 120 Zinc 2 (By similarity). FT METAL 123 123 Zinc 2 (By similarity). FT METAL 131 131 Zinc 2 (By similarity). FT METAL 173 173 Zinc 1; catalytic (By similarity). SQ SEQUENCE 382 AA; 41538 MW; 1006FA596DE91A17 CRC64; MRALAYFKKG DIHFTNDIPR PEIQTDDEVI IDVSWCGICG SDLHEYLDGP IFMPKDGECH KLSNAALPLA MGHEMSGIVS KVGPKVTKVK VGDHVVVDAA SSCADLHCWP HSKFYNSKPC DACQRGSENL CTHAGFVGLG VISGGFAEQV VVSQHHIIPV PKEIPLDVAA LVEPLSVTWH AVKISGFKKG SSALVLGAGP IGLCTILVLK GMGASKIVVS EIAERRIEMA KKLGVEVFNP SKHGHKSIEI LRGLTKSHDG FDYSYDCSGI QVTFETSLKA LTFKGTATNI AVWGPKPVPF QPMDVTLQEK VMTGSIGYVV EAFEEVVRAI HNGDIAMEDC KQLITGKQRI EDGWEKGFQE LMDHKESNVK ILLTPNNHGE MK //