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   25-NOV-2008, entry version 33.
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=BCKDH E1-beta;
DE   Flags: Precursor;
GN   Name=Bckdhb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; 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
RT   subunit of 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex
CC       catalyzes the overall conversion of alpha-keto acids to acyl-CoA
CC       and CO(2). It contains multiple copies of three enzymatic
CC       components: branched-chain alpha-keto acid decarboxylase (E1),
CC       lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
CC   -!- CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate +
CC       [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
CC       lipoyllysine = [dihydrolipoyllysine-residue (2-
CC       methylpropanoyl)transferase] S-(2-
CC       methylpropanoyl)dihydrolipoyllysine + CO(2).
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
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;
CC         Note=No experimental confirmation available;
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DR   EMBL; L16992; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC064099; AAH64099.1; -; mRNA.
DR   RefSeq; NP_954665.1; -.
DR   RefSeq; XP_001481012.1; -.
DR   UniGene; Mm.12819; -.
DR   SMR; Q6P3A8; 1-322.
DR   Ensembl; ENSMUSG00000032263; Mus musculus.
DR   GeneID; 100048676; -.
DR   GeneID; 12040; -.
DR   KEGG; mmu:100048676; -.
DR   KEGG; mmu:12040; -.
DR   MGI; MGI:88137; Bckdhb.
DR   HOGENOM; Q6P3A8; -.
DR   HOVERGEN; Q6P3A8; -.
DR   NextBio; 462083; -.
DR   ArrayExpress; Q6P3A8; -.
DR   GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydroge...; ISS:HGNC.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:MGI.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-me...; IEA:EC.
DR   GO; GO:0003826; F:alpha-ketoacid dehydrogenase activity; IDA:MGI.
DR   GO; GO:0009083; P:branched chain family amino acid catabolic ...; ISS:HGNC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR005476; Transketo_C.
DR   InterPro; IPR005475; Transketo_Cen_R.
DR   InterPro; IPR015941; Transketolase_C-like.
DR   Gene3D; G3DSA:3.40.50.920; Transketo_C_like; 2.
DR   Pfam; PF02779; Transket_pyr; 2.
DR   Pfam; PF02780; Transketolase_C; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT       1     48       Mitochondrion (Potential).
FT   CHAIN        49    390       2-oxoisovalerate dehydrogenase subunit
FT                                beta, mitochondrial.
FT                                /FTId=PRO_0000312367.
FT   VAR_SEQ       1     68       Missing (in isoform 2).
FT                                /FTId=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
//