ODBB_MOUSE
ID ODBB_MOUSE Reviewed; 390 AA.
AC Q6P3A8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit beta, mitochondrial;
DE EC=1.2.4.4;
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component beta chain;
DE Short=BCKDE1B;
DE Short=BCKDH E1-beta;
DE Flags: Precursor;
GN Name=Bckdhb;
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 [MRNA] (ISOFORM 1).
RX PubMed=8268236; DOI=10.1016/0167-4781(93)90023-7;
RA Chinsky J.M., Costeas P.A.;
RT "Molecular cloning and analysis of the expression of the E1 beta subunit of
RT branched chain alpha-ketoacid dehydrogenase in mice.";
RL Biochim. Biophys. Acta 1216:499-503(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230 AND LYS-239, AND
RP IDENTIFICATION BY MASS 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 -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It
CC contains multiple copies of three enzymatic components: branched-chain
CC alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC lipoamide dehydrogenase (E3).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-
CC methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-
CC N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2;
CC Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rhea:RHEA-COMP:10489,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83142; EC=1.2.4.4;
CC -!- SUBUNIT: Heterotetramer of 2 alpha and 2 beta chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P3A8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P3A8-2; Sequence=VSP_029841;
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DR EMBL; L16992; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC064099; AAH64099.1; -; mRNA.
DR CCDS; CCDS23378.1; -. [Q6P3A8-2]
DR CCDS; CCDS81045.1; -. [Q6P3A8-1]
DR RefSeq; NP_001292864.1; NM_001305935.1. [Q6P3A8-1]
DR RefSeq; NP_954665.1; NM_199195.1. [Q6P3A8-2]
DR AlphaFoldDB; Q6P3A8; -.
DR SMR; Q6P3A8; -.
DR BioGRID; 198315; 3.
DR IntAct; Q6P3A8; 1.
DR MINT; Q6P3A8; -.
DR STRING; 10090.ENSMUSP00000139684; -.
DR iPTMnet; Q6P3A8; -.
DR PhosphoSitePlus; Q6P3A8; -.
DR SwissPalm; Q6P3A8; -.
DR EPD; Q6P3A8; -.
DR jPOST; Q6P3A8; -.
DR MaxQB; Q6P3A8; -.
DR PaxDb; Q6P3A8; -.
DR PeptideAtlas; Q6P3A8; -.
DR PRIDE; Q6P3A8; -.
DR ProteomicsDB; 293920; -. [Q6P3A8-1]
DR ProteomicsDB; 293921; -. [Q6P3A8-2]
DR Antibodypedia; 49986; 104 antibodies from 22 providers.
DR DNASU; 12040; -.
DR Ensembl; ENSMUST00000034801; ENSMUSP00000034801; ENSMUSG00000032263. [Q6P3A8-2]
DR Ensembl; ENSMUST00000190166; ENSMUSP00000140598; ENSMUSG00000032263. [Q6P3A8-2]
DR Ensembl; ENSMUST00000190637; ENSMUSP00000139684; ENSMUSG00000032263. [Q6P3A8-1]
DR GeneID; 12040; -.
DR KEGG; mmu:12040; -.
DR UCSC; uc009qwr.1; mouse. [Q6P3A8-1]
DR CTD; 594; -.
DR MGI; MGI:88137; Bckdhb.
DR VEuPathDB; HostDB:ENSMUSG00000032263; -.
DR eggNOG; KOG0525; Eukaryota.
DR GeneTree; ENSGT00940000156533; -.
DR HOGENOM; CLU_012907_1_0_1; -.
DR InParanoid; Q6P3A8; -.
DR OMA; SEAYYMA; -.
DR OrthoDB; 1200844at2759; -.
DR PhylomeDB; Q6P3A8; -.
DR TreeFam; TF105947; -.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
DR BioGRID-ORCS; 12040; 1 hit in 59 CRISPR screens.
DR ChiTaRS; Bckdhb; mouse.
DR PRO; PR:Q6P3A8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6P3A8; protein.
DR Bgee; ENSMUSG00000032263; Expressed in left lobe of liver and 267 other tissues.
DR Genevisible; Q6P3A8; MM.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; ISS:HGNC-UCL.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; ISS:HGNC-UCL.
DR GO; GO:0009063; P:cellular amino acid catabolic process; TAS:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IBA:GO_Central.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Lipid metabolism; Mitochondrion;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 49..390
FT /note="2-oxoisovalerate dehydrogenase subunit beta,
FT mitochondrial"
FT /id="PRO_0000312367"
FT MOD_RES 230
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 239
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029841"
SQ SEQUENCE 390 AA; 42880 MW; 507E04F01BCCD298 CRC64;
MAAVAARAGG LLWLRAAGAE RRRCGLRCAA LVQGFLQPGG EDTAQKRRVA HFTFHPDPES
LQYGQTQKMN LFQSITSALD NSLAKDPTAV IFGEDVAFGG VFRCTVGLRD KYGKDRVFNT
PLCEQGIVGF GIGIAVTGAT AIAEIQFADY IFPAFDQIVN EAAKYRYRSG DLFNCGSLTI
RAPWGCVGHG ALYHSQSPEA FFAHCPGIKV VIPRSPFQAK GLLLSCIEDK NPCIFFEPKI
LYRAAVEQVP VEPYKIPLSQ AEVIQEGSDV TLVAWGTQVH VIREVASMAQ EKLGVSCEVI
DLRTIVPWDV DTVCKSVIKT GRLLISHEAP LTGGFASEIS STVQEECFLN LEAPISRVCG
YDTPFPHIFE PFYIPDKWKC YDALRKMINY
