ID BDH2_MOUSE Reviewed; 245 AA. AC Q8JZV9; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 25-NOV-2008, entry version 47. DE RecName: Full=3-hydroxybutyrate dehydrogenase type 2; DE EC=1.1.1.30; DE AltName: Full=R-beta-hydroxybutyrate dehydrogenase; DE AltName: Full=Dehydrogenase/reductase SDR family member 6; GN Name=Bdh2; Synonyms=Dhrs6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; 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 -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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; BC036998; AAH36998.1; -; mRNA. DR RefSeq; NP_081484.1; -. DR UniGene; Mm.45121; -. DR HSSP; P97852; 1GZ6. DR SMR; Q8JZV9; 1-245. DR PhosphoSite; Q8JZV9; -. DR Ensembl; ENSMUSG00000028167; Mus musculus. DR GeneID; 69772; -. DR KEGG; mmu:69772; -. DR NMPDR; fig|10090.3.peg.9033; -. DR MGI; MGI:1917022; Bdh2. DR HOVERGEN; Q8JZV9; -. DR NextBio; 330302; -. DR ArrayExpress; Q8JZV9; -. DR CleanEx; MM_BDH2; -. DR GermOnline; ENSMUSG00000028167; Mus musculus. DR GO; GO:0005737; C:cytoplasm; ISS:HGNC. DR GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; ISS:HGNC. DR GO; GO:0051287; F:NAD binding; ISS:HGNC. DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:HGNC. 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 2: Evidence at transcript level; KW Cytoplasm; NAD; Oxidoreductase; Phosphoprotein. FT CHAIN 1 245 3-hydroxybutyrate dehydrogenase type 2. FT /FTId=PRO_0000042581. FT NP_BIND 10 37 NAD (By similarity). FT NP_BIND 180 184 NAD (By similarity). FT ACT_SITE 147 147 Proton acceptor (By similarity). FT BINDING 58 58 NAD (By similarity). FT BINDING 144 144 Substrate (By similarity). FT BINDING 151 151 NAD (By similarity). FT BINDING 188 188 Substrate (By similarity). FT BINDING 205 205 Substrate (By similarity). FT MOD_RES 132 132 Phosphoserine (By similarity). SQ SEQUENCE 245 AA; 26753 MW; 343A25B1F56B9CCF CRC64; MGRLDGKVIV LTAAAQGIGR ASALAFAREG AKVIATDINE SKLQELESYR GIQTRVLDVT KKRQIDQFAS EIERIDVLFN VAGFVHHGTI LDCEEKDWDF SMNLNVRSMF LMIKAFLPKM LAQKSGNIIN MSSVASSIKG VENRCVYSAT KAAVIGLTKS VAADFIQQGI RCNCVCPGTV DTPSLQERIQ ARDNPKEALK TFLNRQKTGR FASAEEVALL CVYLASDESA YVTGNPVIID GGWSL //