P50136
uniprot
P50136
canonical
amino_acid_sequence
MSAAKIWRPSRGLRQAALLLLGRSGVRGLARSHPSRQQQQQFPSLDDKPQFPGASAEFVDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPQEEVLKFYRSMTLLNTMDRILYESQREGRISFYMTNYGEEGTHVGSAAALERTDLVFGQYREAGVLMYRDYPLELFMSQCYGNVNDPGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRIVICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIKSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHPISRLRQYLLNQGWWDEEQEKAWRKQSRKKVMEAFEQAERKLKPNPSLLFSDVYQEMPAQLRRQQESLARHLQTYGEHYPLDHFEK
uniprot
proteins
ec_number
1.2.4.4
uniprot
proteins
function
FUNCTION: Together with BCKDHB forms the heterotetrameric E1 subunit of the mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD) complex. The BCKD complex catalyzes the multi-step oxidative decarboxylation of alpha-ketoacids derived from the branched-chain amino-acids valine, leucine and isoleucine producing CO2 and acyl-CoA which is subsequently utilized to produce energy. The E1 subunit catalyzes the first step with the decarboxylation of the alpha-ketoacid forming an enzyme-product intermediate. A reductive acylation mediated by the lipoylamide cofactor of E2 extracts the acyl group from the E1 active site for the next step of the reaction. {ECO:0000250|UniProtKB:P12694}.
uniprot
proteins
mass_dalton
50371
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-334 by BCKDK and dephosphorylated by protein phosphatase PPM1K. {ECO:0000250|UniProtKB:P12694}.
uniprot
proteins
protein_family
BCKDHA family
uniprot
proteins
pubmed
17208939
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23576753
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
8761456
uniprot
proteins
sequence_length
442
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P12694}.
uniprot
proteins