BDH_MESAU
ID BDH_MESAU Reviewed; 132 AA.
AC P86198;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 43.
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: Fragments;
GN Name=BDH1 {ECO:0000250|UniProtKB:Q02338};
GN Synonyms=BDH {ECO:0000250|UniProtKB:Q02338};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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:0000255}.
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DR AlphaFoldDB; P86198; -.
DR SMR; P86198; -.
DR PRIDE; P86198; -.
DR Proteomes; UP000189706; Unplaced.
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; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; Glycoprotein; Lipid metabolism; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT CHAIN <1..>132
FT /note="D-beta-hydroxybutyrate dehydrogenase, mitochondrial"
FT /id="PRO_0000394393"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q02338,
FT ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 3..27
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q02338"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02338"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XN0"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29147"
FT CARBOHYD 77
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT NON_CONS 33..34
FT /evidence="ECO:0000305"
FT NON_CONS 45..46
FT /evidence="ECO:0000305"
FT NON_CONS 53..54
FT /evidence="ECO:0000305"
FT NON_CONS 63..64
FT /evidence="ECO:0000305"
FT NON_CONS 110..111
FT /evidence="ECO:0000305"
FT NON_CONS 121..122
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 132
SQ SEQUENCE 132 AA; 15007 MW; 5BEE8D8BF102E584 CRC64;
AVLVTGCDSG FGFSLAKHLH SKGFLVFAGC LLKEVAEVNL WGTVRSFLPL LRRVVNISSM
LGRSPYCITK FGVEAFSDCL RYEMHPLGVK VSVVEPGNFI AATSLYSPER MWDELPEVVR
KYHPMDYYWW LR
