BDH_MOUSE
ID BDH_MOUSE Reviewed; 343 AA.
AC Q80XN0; Q3UJS9; Q3UL45; Q8BK53; Q8R0C8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
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:0000312|MGI:MGI:1919161};
GN Synonyms=Bdh {ECO:0000250|UniProtKB:Q02338};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Liver;
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 PROTEIN SEQUENCE OF 224-252, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-103 AND LYS-259, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-97; LYS-103; LYS-132;
RP LYS-177; LYS-212; LYS-258; LYS-259 AND LYS-280, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(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: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 -!- PTM: Acetylation of Lys-132 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AK076718; BAC36453.1; -; mRNA.
DR EMBL; AK137955; BAE23523.1; -; mRNA.
DR EMBL; AK145711; BAE26605.1; -; mRNA.
DR EMBL; AK146321; BAE27076.1; -; mRNA.
DR EMBL; BC027063; AAH27063.1; -; mRNA.
DR EMBL; BC043683; AAH43683.1; -; mRNA.
DR EMBL; BC096457; AAH96457.1; -; mRNA.
DR CCDS; CCDS28106.1; -.
DR RefSeq; NP_001116155.1; NM_001122683.1.
DR RefSeq; NP_780386.3; NM_175177.4.
DR AlphaFoldDB; Q80XN0; -.
DR SMR; Q80XN0; -.
DR BioGRID; 215024; 8.
DR IntAct; Q80XN0; 3.
DR STRING; 10090.ENSMUSP00000110882; -.
DR GlyGen; Q80XN0; 1 site.
DR iPTMnet; Q80XN0; -.
DR PhosphoSitePlus; Q80XN0; -.
DR SwissPalm; Q80XN0; -.
DR EPD; Q80XN0; -.
DR jPOST; Q80XN0; -.
DR MaxQB; Q80XN0; -.
DR PaxDb; Q80XN0; -.
DR PeptideAtlas; Q80XN0; -.
DR PRIDE; Q80XN0; -.
DR ProteomicsDB; 265169; -.
DR Antibodypedia; 33961; 249 antibodies from 30 providers.
DR DNASU; 71911; -.
DR Ensembl; ENSMUST00000089759; ENSMUSP00000087192; ENSMUSG00000046598.
DR Ensembl; ENSMUST00000115226; ENSMUSP00000110881; ENSMUSG00000046598.
DR Ensembl; ENSMUST00000115227; ENSMUSP00000110882; ENSMUSG00000046598.
DR GeneID; 71911; -.
DR KEGG; mmu:71911; -.
DR UCSC; uc007yxi.2; mouse.
DR CTD; 622; -.
DR MGI; MGI:1919161; Bdh1.
DR VEuPathDB; HostDB:ENSMUSG00000046598; -.
DR eggNOG; KOG1610; Eukaryota.
DR GeneTree; ENSGT00940000156929; -.
DR HOGENOM; CLU_010194_2_0_1; -.
DR InParanoid; Q80XN0; -.
DR OMA; FAGCFLK; -.
DR OrthoDB; 1390068at2759; -.
DR PhylomeDB; Q80XN0; -.
DR TreeFam; TF325617; -.
DR Reactome; R-MMU-77108; Utilization of Ketone Bodies.
DR Reactome; R-MMU-77111; Synthesis of Ketone Bodies.
DR BioGRID-ORCS; 71911; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Bdh1; mouse.
DR PRO; PR:Q80XN0; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q80XN0; protein.
DR Bgee; ENSMUSG00000046598; Expressed in embryonic brain and 261 other tissues.
DR ExpressionAtlas; Q80XN0; baseline and differential.
DR Genevisible; Q80XN0; MM.
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; HDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
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:0000250"
FT CHAIN 47..343
FT /note="D-beta-hydroxybutyrate dehydrogenase, mitochondrial"
FT /id="PRO_0000031961"
FT ACT_SITE 209
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 60..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 103
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 103
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 132
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29147"
FT MOD_RES 258
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 259
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 259
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 280
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CARBOHYD 219
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CONFLICT 152
FT /note="E -> G (in Ref. 1; BAC36453)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="I -> V (in Ref. 1; BAC36453/BAE23523/BAE26605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 38299 MW; B72B0550713EDB7F CRC64;
MLAARLSRPL SQLPGKALSV RDRENGTRHT LLFYPASFSP DTRRTYASQA DAASGKAILI
TGCDSGFGFS LAKHLHSKGF LVFAGCLMKD KGDAGVKELD SLKSDRLRTI QLNVCNSEEV
EKAVETIRSG LKDPEKGMWG LVNNAGISTF GEVEFTSMET YKEVAEVNLW GTVRTTKSFL
PLLRRAKGRV VNISSMLGRM ANPARSPYCI TKFGIEAFSD CLRYEMHPLG VKVSVVEPGN
FIAATSLYSP ERIQAIAKKM WDDLPEVVRK DYGRKYFDEK IAKMETYCNS GSTDTSSVIN
AVTHALTAAT PYTRYHPMDY YWWLRMQIMT HFPGAISDKI YIH
