ID BDH_RAT Reviewed; 343 AA. AC P29147; Q5U2Q2; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 2. DT 25-NOV-2008, entry version 70. DE RecName: Full=D-beta-hydroxybutyrate dehydrogenase, mitochondrial; DE Short=BDH; DE EC=1.1.1.30; DE AltName: Full=3-hydroxybutyrate dehydrogenase; DE Flags: Precursor; GN Name=Bdh1; Synonyms=Bdh; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX MEDLINE=92232670; PubMed=1567834; DOI=10.1021/bi00130a009; RA Churchill P., Hempel J., Romovacek H., Zhang W.W., Churchill S., RA Brennan M.; RT "Primary structure of rat liver D-beta-hydroxybutyrate dehydrogenase RT from cDNA and protein analyses: a short-chain alcohol dehydrogenase."; RL Biochemistry 31:3793-3799(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: (R)-3-hydroxybutanoate + NAD(+) = acetoacetate CC + NADH. CC -!- ENZYME REGULATION: Requires phosphatidylcholine as an allosteric CC activator for enzymatic activity (By similarity). CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) 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; M89902; AAB59684.1; ALT_INIT; mRNA. DR EMBL; BC085916; AAH85916.1; ALT_INIT; mRNA. DR PIR; A42345; A42345. DR RefSeq; NP_446447.2; -. DR UniGene; Rn.36635; -. DR HSSP; P14061; 1FDS. DR Ensembl; ENSRNOG00000001736; Rattus norvegicus. DR GeneID; 117099; -. DR KEGG; rno:117099; -. DR NMPDR; fig|10116.3.peg.7406; -. DR RGD; 620131; Bdh1. DR HOVERGEN; P29147; -. DR NextBio; 619980; -. DR ArrayExpress; P29147; -. DR GermOnline; ENSRNOG00000001736; Rattus norvegicus. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; IEA:EC. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002198; DHase_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DHase. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR19410; ADH_short_C2; 1. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Acetylation; Allosteric enzyme; Direct protein sequencing; KW Mitochondrion; NAD; Oxidoreductase; Transit peptide. FT TRANSIT 1 46 Mitochondrion. FT CHAIN 47 343 D-beta-hydroxybutyrate dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000031962. FT NP_BIND 59 83 NAD (By similarity). FT ACT_SITE 208 208 Proton acceptor (By similarity). FT BINDING 195 195 Substrate (By similarity). FT MOD_RES 132 132 N6-acetyllysine (By similarity). FT MOD_RES 275 275 N6-acetyllysine (By similarity). FT CONFLICT 90 91 DK -> EQ (in Ref. 1; AAB59684). SQ SEQUENCE 343 AA; 38202 MW; 6903D2ED27F2B055 CRC64; MLAARLSRPL SQLPGKALSV CDRENGTRHT LLFYPASFSP DTRRTYTSQA DAASGKAVLV TGCDSGFGFS LAKHLHSKGF LVFAGCLLKD KGDAGVRELD SLKSDRLRTI QLNVCNSEEV EKAVETVRSG LKDPEKGMWG LVNNAGISTF GEVEFTSMET YKEVAEVNLW GTVRTTKSFL PLLRRAKGRV VNISSMLGRM ANPARSPYCI TKFGVEAFSD CLRYEMHPLG VKVSVVEPGN FIAATSLYSP ERIQAIAKKM WDELPEVVRK DYGKKYFDEK IAKMETYCNS GSTDTSSVIN AVTHALTAAT PYTRYHPMDY YWWLRMQVMT HFPGAISDKI YIH //