BDH_RAT
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 03-AUG-2022, entry version 157.
DE RecName: Full=D-beta-hydroxybutyrate dehydrogenase, mitochondrial {ECO:0000305};
DE EC=1.1.1.30 {ECO:0000269|PubMed:1567834};
DE AltName: Full=3-hydroxybutyrate dehydrogenase {ECO:0000303|PubMed:1567834};
DE Short=BDH {ECO:0000303|PubMed:1567834};
DE Flags: Precursor;
GN Name=Bdh1 {ECO:0000312|RGD:620131};
GN Synonyms=Bdh {ECO:0000303|PubMed:1567834};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY,
RP AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX 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 from
RT 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=8515054; DOI=10.1177/41.7.8515054;
RA Racine L., Scoazec J.Y., Moreau A., Bernuau D., Feldmann G.;
RT "Effects of digitonin on the intracellular content of rat hepatocytes:
RT implications for its use in the study of intralobular heterogeneity.";
RL J. Histochem. Cytochem. 41:991-1001(1993).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP GLYCOSYLATION AT SER-219.
RX PubMed=24098488; DOI=10.1371/journal.pone.0076399;
RA Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
RT "Discovery and confirmation of O-GlcNAcylated proteins in rat liver
RT mitochondria by combination of mass spectrometry and immunological
RT methods.";
RL PLoS ONE 8:E76399-E76399(2013).
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:0000269|PubMed:1567834};
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:0000269|PubMed:8515054}. Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q02337}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:1567834}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB59684.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH85916.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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; NM_053995.3.
DR RefSeq; XP_006248540.1; XM_006248478.3.
DR RefSeq; XP_008766913.1; XM_008768691.2.
DR AlphaFoldDB; P29147; -.
DR SMR; P29147; -.
DR BioGRID; 250672; 2.
DR IntAct; P29147; 2.
DR MINT; P29147; -.
DR STRING; 10116.ENSRNOP00000002366; -.
DR CarbonylDB; P29147; -.
DR GlyGen; P29147; 1 site.
DR iPTMnet; P29147; -.
DR PhosphoSitePlus; P29147; -.
DR jPOST; P29147; -.
DR PaxDb; P29147; -.
DR PRIDE; P29147; -.
DR GeneID; 117099; -.
DR KEGG; rno:117099; -.
DR UCSC; RGD:620131; rat.
DR CTD; 622; -.
DR RGD; 620131; Bdh1.
DR eggNOG; KOG1610; Eukaryota.
DR InParanoid; P29147; -.
DR OMA; FAGCFLK; -.
DR OrthoDB; 1390068at2759; -.
DR PhylomeDB; P29147; -.
DR TreeFam; TF325617; -.
DR Reactome; R-RNO-77108; Utilization of Ketone Bodies.
DR Reactome; R-RNO-77111; Synthesis of Ketone Bodies.
DR SABIO-RK; P29147; -.
DR PRO; PR:P29147; -.
DR Proteomes; UP000002494; 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:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; IDA:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IDA:RGD.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0060612; P:adipose tissue development; IEP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0060416; P:response to growth hormone; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 CHAIN 47..343
FT /note="D-beta-hydroxybutyrate dehydrogenase, mitochondrial"
FT /id="PRO_0000031962"
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 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 132
FT /note="N6-acetyllysine"
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:0007744|PubMed:22673903"
FT MOD_RES 258
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 259
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 259
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 280
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT CARBOHYD 219
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:24098488"
FT CONFLICT 90..91
FT /note="DK -> EQ (in Ref. 1; AAB59684)"
FT /evidence="ECO:0000305"
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
