Pdhb
entrez
68263
canonical
uniprot
Q9D051
canonical
ensembl
ENSMUSG00000021748
resolver
ensp
ENSMUSP00000022268
resolver
enst
ENSMUST00000022268
resolver
genesymbol
Pdhb
resolver
uniprot
Q3TL86
resolver
uniprot
Q505N8
resolver
uniprot
Q99LW9
resolver
uniprot_entry
ODPB_MOUSE
resolver
uniprot_sec
Q3TL86
resolver
uniprot_sec
Q505N8
resolver
uniprot_sec
Q99LW9
resolver
amino_acid_sequence
MAVVAGLVRGPLRQASGLLKRRFHRSAPAAVQLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVMLENELMYGVAFELPAEAQSKDFLIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKVLEDNSVPQVKDIIFAVKKTLNI
uniprot
proteins
ec_number
1.2.4.1
uniprot
proteins
function
FUNCTION: Together with PDHA1 forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex. The PDH complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3). The E1 subunit catalyzes both the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvate and the reductive acetylation of a lipoyl group covalently linked to the lipoyl-bearing domains of E2. {ECO:0000250|UniProtKB:P11177}.
uniprot
proteins
mass_dalton
38937
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18034455
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23576753
uniprot
proteins
sequence_length
359
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P26284}.
uniprot
proteins