BDH_BOVIN
ID BDH_BOVIN Reviewed; 344 AA.
AC Q02337; Q3ZBX3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=D-beta-hydroxybutyrate dehydrogenase, mitochondrial {ECO:0000305};
DE EC=1.1.1.30 {ECO:0000250|UniProtKB:P29147};
DE AltName: Full=3-hydroxybutyrate dehydrogenase {ECO:0000303|PubMed:1639787};
DE Short=BDH {ECO:0000303|PubMed:1639787};
DE Flags: Precursor;
GN Name=BDH1 {ECO:0000250|UniProtKB:Q02338};
GN Synonyms=BDH {ECO:0000303|PubMed:1639787};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 47-89; 138-174; 213-231; 233-259; 285-322 AND 331-344.
RC TISSUE=Heart;
RX PubMed=1639787; DOI=10.1016/s0021-9258(19)49556-2;
RA Marks A.R., McIntyre J.O., Duncan T.M., Erdjument-Bromage H., Tempst P.,
RA Fleischer S.;
RT "Molecular cloning and characterization of (R)-3-hydroxybutyrate
RT dehydrogenase from human heart.";
RL J. Biol. Chem. 267:15459-15463(1992).
RN [3]
RP PROTEIN SEQUENCE OF 163-174 AND 285-301.
RC TISSUE=Heart;
RX PubMed=3527172;
RA Prasad P.V., Hatefi Y.;
RT "Amino acid sequences of two tryptic peptides from D(-)-beta-
RT hydroxybutyrate dehydrogenase radiolabeled at essential carboxyl and
RT sulfhydryl groups.";
RL Biochem. Int. 12:941-949(1986).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=718894; DOI=10.1016/0005-2736(78)90178-5;
RA McIntyre J.O., Bock H.G., Fleischer S.;
RT "The orientation of D-beta-hydroxybutyrate dehydrogenase in the
RT mitochondrial inner membrane.";
RL Biochim. Biophys. Acta 513:255-267(1978).
RN [5]
RP SUBUNIT.
RX PubMed=6822516; DOI=10.1016/s0021-9258(18)33143-0;
RA McIntyre J.O., Churchill P., Maurer A., Berenski C.J., Jung C.Y.,
RA Fleischer S.;
RT "Target size of D-beta-hydroxybutyrate dehydrogenase. Functional and
RT structural molecular weight based on radiation inactivation.";
RL J. Biol. Chem. 258:953-959(1983).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=2550053; DOI=10.1021/bi00439a007;
RA Rudy B., Dubois H., Mink R., Trommer W.E., McIntyre J.O., Fleischer S.;
RT "Coenzyme binding by 3-hydroxybutyrate dehydrogenase, a lipid-requiring
RT enzyme: lecithin acts as an allosteric modulator to enhance the affinity
RT for coenzyme.";
RL Biochemistry 28:5354-5366(1989).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-3-hydroxybutanoate + NAD(+) = acetoacetate + H(+) + NADH;
CC Xref=Rhea:RHEA:20521, ChEBI:CHEBI:10983, ChEBI:CHEBI:13705,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.30;
CC Evidence={ECO:0000250|UniProtKB:P29147};
CC -!- ACTIVITY REGULATION: Requires phosphatidylcholine as an allosteric
CC activator for enzymatic activity. {ECO:0000269|PubMed:2550053}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:6822516}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:718894}. Mitochondrion matrix
CC {ECO:0000269|PubMed:718894}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BC103051; AAI03052.1; -; mRNA.
DR PIR; B42845; B42845.
DR RefSeq; NP_001029772.1; NM_001034600.2.
DR RefSeq; XP_005201561.3; XM_005201504.3.
DR RefSeq; XP_005201562.1; XM_005201505.3.
DR AlphaFoldDB; Q02337; -.
DR SMR; Q02337; -.
DR STRING; 9913.ENSBTAP00000000573; -.
DR PaxDb; Q02337; -.
DR PeptideAtlas; Q02337; -.
DR PRIDE; Q02337; -.
DR Ensembl; ENSBTAT00000000573; ENSBTAP00000000573; ENSBTAG00000000448.
DR Ensembl; ENSBTAT00000082799; ENSBTAP00000065955; ENSBTAG00000000448.
DR GeneID; 534090; -.
DR KEGG; bta:534090; -.
DR CTD; 622; -.
DR VEuPathDB; HostDB:ENSBTAG00000000448; -.
DR VGNC; VGNC:26457; BDH1.
DR eggNOG; KOG1610; Eukaryota.
DR GeneTree; ENSGT00940000156929; -.
DR HOGENOM; CLU_010194_2_0_1; -.
DR InParanoid; Q02337; -.
DR OMA; FAGCFLK; -.
DR OrthoDB; 1390068at2759; -.
DR TreeFam; TF325617; -.
DR Reactome; R-BTA-77108; Utilization of Ketone Bodies.
DR Reactome; R-BTA-77111; Synthesis of Ketone Bodies.
DR SABIO-RK; Q02337; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000000448; Expressed in ruminant reticulum and 106 other tissues.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0099617; C:matrix side of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
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 Acetylation; Allosteric enzyme; Direct protein sequencing; Glycoprotein;
KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1639787"
FT CHAIN 47..344
FT /note="D-beta-hydroxybutyrate dehydrogenase, mitochondrial"
FT /id="PRO_0000054526"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 59..83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 103
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 103
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29147"
FT MOD_RES 260
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 260
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 281
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT CARBOHYD 219
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 344 AA; 38391 MW; C8C7AC75FA09880E CRC64;
MLTARLSRPL SQLPRKTLNF SDRENGTRGS LLLYSAPFVP VGRRTYAASV DPVGSKAVLI
TGCDSGFGFS LAKHLHSEGF LVFAGCLMKD KGSDGVKELD SMKSDRLRTV QLNVCKSEEV
DKAAEVIRSS LEDPEKGLWG LVNNAGISTF GDVEFTSMET YKEVAEVNLW GTVRVTKAFL
PLIRRAKGRV VNISSMMGRM ANVARSPYCI TKFGVEAFSD CLRYEMHPLG VKVSVVEPGN
FIAATSLYGG TERIQAIANK MWEELPEVVR QDYGRKYFDE KVARMESYCT SGSTDTSPVI
KAVTHALTAT TPYTRYHPMD YYWWLRMQIM THFPGAISDR IYIH
