ID   BDH_CHICK               Reviewed;         339 AA.
AC   Q5ZJZ5;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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:0000250|UniProtKB:Q02338};
DE            Short=BDH {ECO:0000250|UniProtKB:Q02338};
DE   Flags: Precursor;
GN   Name=BDH1 {ECO:0000250|UniProtKB:Q02338};
GN   Synonyms=BDH {ECO:0000250|UniProtKB:Q02338};
GN   ORFNames=RCJMB04_14d17 {ECO:0000312|EMBL:CAG31948.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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:0000250|UniProtKB:Q02337}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q02337}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q02337}. Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q02337}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AJ720289; CAG31948.1; -; mRNA.
DR   AlphaFoldDB; Q5ZJZ5; -.
DR   SMR; Q5ZJZ5; -.
DR   BioGRID; 685209; 1.
DR   STRING; 9031.ENSGALP00000011241; -.
DR   PaxDb; Q5ZJZ5; -.
DR   VEuPathDB; HostDB:geneid_424891; -.
DR   eggNOG; KOG1610; Eukaryota.
DR   InParanoid; Q5ZJZ5; -.
DR   PhylomeDB; Q5ZJZ5; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0099617; C:matrix side of mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Allosteric enzyme; Lipid metabolism; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..46
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           47..339
FT                   /note="D-beta-hydroxybutyrate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000031963"
FT   ACT_SITE        204
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  38237 MW;  208BADB539C6F108 CRC64;
     MLATKLSRPL LNLPVKTLTV KNPGNSFRPV QRFCFPLLSS CGSRSYASEV DQIGSRAVLT
     LGLDLPWPKH LHTKGFIIYA GCLQKNKGEG GSKDLDNMNS DRMRTVQLNV CDSKEVDRAV
     EHVNSSLEDP EKGLWGLVNN AGISTFGEVE FTSMDTYMEV AEVNLWGTVR TTKAFLPLIR
     RSKGRVVNIS SMMGRMGSPA RSPYCITKFG VEAFSDCLRY EMQPQGVMVS IVEPGNFIAV
     TNLYSPERIK AIADKMWDEL PEIVRKDYGR KYFDEQVSKM ETYCNSGSTD TSPVIESVAH
     ALTSTAPYTR YHPMDYYWWL RMQIMTHMPA AISDRLYVY