ID   ODBA_RAT                Reviewed;         441 AA.
AC   P11960;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial;
DE            EC=1.2.4.4;
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain;
DE            Short=BCKDE1A;
DE            Short=BCKDH E1-alpha;
DE   Flags: Precursor; Fragment;
GN   Name=Bckdha;
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].
RX   PubMed=2822716; DOI=10.1016/s0021-9258(18)48161-6;
RA   Zhang B., Kuntz M.J., Goodwin G.W., Harris R.A., Crabb D.W.;
RT   "Molecular cloning of a cDNA for the E1 alpha subunit of rat liver branched
RT   chain alpha-ketoacid dehydrogenase.";
RL   J. Biol. Chem. 262:15220-15224(1987).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16396499; DOI=10.1021/pr0503073;
RA   Moser K., White F.M.;
RT   "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT   MS/MS.";
RL   J. Proteome Res. 5:98-104(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-343, AND
RP   IDENTIFICATION BY 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).
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC   -!- SUBUNIT: Heterotetramer of alpha and beta chains. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- MISCELLANEOUS: Bound potassium ions stabilize the protein structure.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BCKDHA family. {ECO:0000305}.
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DR   EMBL; J02827; AAA40811.1; -; mRNA.
DR   PIR; A29468; DERTXA.
DR   RefSeq; NP_036914.1; NM_012782.1.
DR   AlphaFoldDB; P11960; -.
DR   SMR; P11960; -.
DR   BioGRID; 247284; 3.
DR   IntAct; P11960; 3.
DR   MINT; P11960; -.
DR   STRING; 10116.ENSRNOP00000027995; -.
DR   iPTMnet; P11960; -.
DR   PhosphoSitePlus; P11960; -.
DR   jPOST; P11960; -.
DR   PaxDb; P11960; -.
DR   PRIDE; P11960; -.
DR   GeneID; 25244; -.
DR   KEGG; rno:25244; -.
DR   UCSC; RGD:2196; rat.
DR   CTD; 593; -.
DR   RGD; 2196; Bckdha.
DR   eggNOG; KOG1182; Eukaryota.
DR   InParanoid; P11960; -.
DR   OrthoDB; 623111at2759; -.
DR   PhylomeDB; P11960; -.
DR   Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-RNO-70895; Branched-chain amino acid catabolism.
DR   SABIO-RK; P11960; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; ISS:HGNC-UCL.
DR   GO; GO:0005739; C:mitochondrion; TAS:RGD.
DR   GO; GO:0047101; F:2-oxoisovalerate dehydrogenase (acylating) activity; TAS:RGD.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; ISS:HGNC-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; ISS:HGNC-UCL.
DR   GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR   GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR   InterPro; IPR034616; BCKDH_E1-a.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   PANTHER; PTHR43380:SF1; PTHR43380:SF1; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein;
KW   Potassium; Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         <1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           42..441
FT                   /note="2-oxoisovalerate dehydrogenase subunit alpha,
FT                   mitochondrial"
FT                   /id="PRO_0000020468"
FT   BINDING         153..155
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         334
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P50136"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50136"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16396499,
FT                   ECO:0007744|PubMed:22673903"
FT   MOD_RES         352
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50136"
FT   MOD_RES         352
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P50136"
FT   MOD_RES         376
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50136"
FT   NON_TER         1
SQ   SEQUENCE   441 AA;  50164 MW;  FFD7709A94094C8E CRC64;
     SAAKIWRPSR GLRQAALLLL GRPGARGLAR FHPSRQQQQQ FPSLDDKPQF PGASAEFVDK
     LEFIQPNVIS GIPIYRVMDR QGQIINPSED PHLPQEEVLK LYRSMTLLNT MDRILYESQR
     QGRISFYMTN YGEEGTHVGS AAALERTDLV FGQYREAGVL MYRDYPLELF MAQCYGNVSD
     PGKGRQMPVH YGCKERHFVT ISSPLATQIP QAVGAAYAAK RANANQIVIC YFGEGAASEG
     DAHAGFNFAA TLECPIIFFC RNNGYAISTP TSEQYRGDGI AARGPGYGIM SIRVDGNDVF
     AVYNATKEAR RRAVAENQPF LIEAMTYRIG HHSTSDDSSA YRSVDEVNYW DKQDHPISRL
     RQYLLNQGWW DEEQEKAWRK QSRKKVMEAF EQAERKLKPN PSLLFSDVYQ EMPAQLRRQQ
     ESLARHLQTY GEHYPLDHFD K