Bckdk
entrez
29603
canonical
uniprot
Q00972
canonical
ensembl
ENSRNOG00000077965
resolver
ensembl
ENSRNOG00055029958
resolver
ensembl
ENSRNOG00065015374
resolver
ensp
ENSRNOP00000069014
resolver
ensp
ENSRNOP00055042864
resolver
ensp
ENSRNOP00065020009
resolver
enst
ENSRNOT00000078578
resolver
enst
ENSRNOT00055051927
resolver
enst
ENSRNOT00065025493
resolver
genesymbol
Bckdk
resolver
uniprot
Q64552
resolver
uniprot_entry
BCKD_RAT
resolver
uniprot_sec
Q64552
resolver
activity_regulation
ACTIVITY REGULATION: The ATP-ase activity is up-regulated by potassium and rubidium ions but not by sodium ions. Up-regulated in the presence of apo- or lipoylated-DBT/E2b subunit of the BCKDH complex. {ECO:0000269|PubMed:11562470}.
uniprot
proteins
amino_acid_sequence
MILTSVLGSGPRSGSSLWPLLGSSLSLRVRSTSATDTHHVELARERSKTVTSFYNQSAIDVVAEKPSVRLTPTMMLYSGRSQDGSHLLKSGRYLQQELPVRIAHRIKGFRSLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIEDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRISPLFGHLDMHSGGQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
ec_number
2.7.11.4
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase component of macronutrients metabolism. Forms a functional kinase and phosphatase pair with PPM1K, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial BCKDHA subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and cytosolic ACLY, a lipogenic enzyme of Krebs cycle (Probable) (PubMed:1377677, PubMed:7649998). Phosphorylates and inactivates mitochondrial BCKDH complex a multisubunit complex consisting of three multimeric components each involved in different steps of BCAA catabolism: E1 composed of BCKDHA and BCKDHB, E2 core composed of DBT monomers, and E3 composed of DLD monomers. Associates with the E2 component of BCKDH complex and phosphorylates BCKDHA on Ser-333, leading to conformational changes that interrupt substrate channeling between E1 and E2 and inactivates the BCKDH complex (Probable) (PubMed:1377677, PubMed:7649998). phosphorylates ACLY on Ser-455 in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and glucogenesis, respectively (Probable). Recognizes phosphosites having SxxE/D canonical motif (By similarity). {ECO:0000250|UniProtKB:O14874, ECO:0000269|PubMed:1377677, ECO:0000269|PubMed:7649998, ECO:0000305|PubMed:29779826}.
uniprot
proteins
mass_dalton
46474
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated. {ECO:0000269|PubMed:7649998}.
uniprot
proteins
protein_family
PDK/BCKDK protein kinase family
uniprot
proteins
pubmed
11562470
uniprot
proteins
pubmed
1377677
uniprot
proteins
pubmed
1496922
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
29779826
uniprot
proteins
pubmed
7649998
uniprot
proteins
sequence_length
412
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion {ECO:0000269|PubMed:29779826}. Note=Detected in the cytosolic compartment of liver cells. {ECO:0000269|PubMed:29779826}.
uniprot
proteins