ODBA_BOVIN
ID ODBA_BOVIN Reviewed; 455 AA.
AC P11178;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 132.
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;
GN Name=BCKDHA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3379058; DOI=10.1016/s0021-9258(18)68408-x;
RA Hu C.-W.C., Lau K.S., Griffin T.A., Chuang J.L., Fisher C.W., Cox R.P.,
RA Chuang D.T.;
RT "Isolation and sequencing of a cDNA encoding the decarboxylase (E1)alpha
RT precursor of bovine branched-chain alpha-keto acid dehydrogenase complex.
RT Expression of E1 alpha mRNA and subunit in maple-syrup-urine-disease and
RT 3T3-L1 cells.";
RL J. Biol. Chem. 263:9007-9014(1988).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CHARACTERIZATION OF
RP COMPLEX CATALYTIC ACTIVITY.
RX PubMed=283398; DOI=10.1073/pnas.75.10.4881;
RA Pettit F.H., Yeaman S.J., Reed L.J.;
RT "Purification and characterization of branched chain alpha-keto acid
RT dehydrogenase complex of bovine kidney.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:4881-4885(1978).
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). {ECO:0000269|PubMed:283398}.
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 {ECO:0000269|PubMed:283398}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney (at protein level).
CC {ECO:0000269|PubMed:283398}.
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; J03759; AAA30595.1; -; mRNA.
DR PIR; A28073; DEBOXA.
DR RefSeq; NP_776931.1; NM_174506.1.
DR AlphaFoldDB; P11178; -.
DR SMR; P11178; -.
DR IntAct; P11178; 1.
DR STRING; 9913.ENSBTAP00000021342; -.
DR PaxDb; P11178; -.
DR PRIDE; P11178; -.
DR GeneID; 282149; -.
DR KEGG; bta:282149; -.
DR CTD; 593; -.
DR eggNOG; KOG1182; Eukaryota.
DR InParanoid; P11178; -.
DR OrthoDB; 623111at2759; -.
DR SABIO-RK; P11178; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IBA:GO_Central.
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..55
FT /note="Mitochondrion"
FT CHAIN 56..455
FT /note="2-oxoisovalerate dehydrogenase subunit alpha,
FT mitochondrial"
FT /id="PRO_0000020464"
FT BINDING 167..169
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50136"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P50136"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50136"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50136"
FT MOD_RES 366
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P50136"
FT MOD_RES 366
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P50136"
FT MOD_RES 390
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50136"
SQ SEQUENCE 455 AA; 51678 MW; 66A7CA6003E0B846 CRC64;
MQGSAKMAMA VAVAVARVWR PSRGLGRTGL PLLRLLGARG LARFHPHRWQ QQQHFSSLDD
KPQFPGASAE FIDKLEFIQP NVISGIPIYR VMDRQGQIIN PSEDPHLPQE KVLKFYKSMT
LLNTMDRILY ESQRQGRISF YMTNYGEEGT HVGSAAALDD TDLVFGQYRE AGVLMYRDYP
LELFMAQCYG NVSDLGKGRQ MPVHYGCRER HFVTISSPLA TQIPQAVGAA YAAKRANANR
VVICYFGEGA ASEGDAHAGF NFAATLECPI IFFCRNNGYA ISTPTSEQYR GDGIAARGPG
YGILSIRVDG NDVFAVYNAT KEARRRAVAE NQPFLIEAMT YRIGHHSTSD DSSAYRSVDE
VNYWDKQDHP ISRLRHHLQS RGWWDDEQEK AWRKQSRKKV MEAFEQAERK LKPNPSLIFS
DVYQEMPAQL RKQQESLARH LQTYGEHYPL DHFEK
