BCKD_BOVIN
ID BCKD_BOVIN Reviewed; 412 AA.
AC Q2KJG8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial;
DE EC=2.7.11.4;
DE AltName: Full=Branched-chain alpha-ketoacid dehydrogenase kinase;
DE Short=BCKD-kinase;
DE Short=BCKDHKIN;
DE Flags: Precursor;
GN Name=BCKDK;
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 [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation and inactivation of the
CC branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory
CC enzyme of the valine, leucine and isoleucine catabolic pathways. Key
CC enzyme that regulate the activity state of the BCKD complex.
CC {ECO:0000250|UniProtKB:O14874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] = ADP +
CC H(+) + O-phospho-L-seryl-[3-methyl-2-oxobutanoate dehydrogenase];
CC Xref=Rhea:RHEA:17301, Rhea:RHEA-COMP:13695, Rhea:RHEA-COMP:13696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.4;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Mitochondrion
CC {ECO:0000250|UniProtKB:O14874}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O14874}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000305}.
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DR EMBL; BC105352; AAI05353.1; -; mRNA.
DR RefSeq; NP_001039371.1; NM_001045906.2.
DR AlphaFoldDB; Q2KJG8; -.
DR SMR; Q2KJG8; -.
DR STRING; 9913.ENSBTAP00000013909; -.
DR PaxDb; Q2KJG8; -.
DR PRIDE; Q2KJG8; -.
DR Ensembl; ENSBTAT00000013909; ENSBTAP00000013909; ENSBTAG00000010524.
DR Ensembl; ENSBTAT00000068647; ENSBTAP00000067306; ENSBTAG00000010524.
DR GeneID; 505005; -.
DR KEGG; bta:505005; -.
DR CTD; 10295; -.
DR VEuPathDB; HostDB:ENSBTAG00000010524; -.
DR VGNC; VGNC:26444; BCKDK.
DR eggNOG; KOG0787; Eukaryota.
DR GeneTree; ENSGT01030000234646; -.
DR HOGENOM; CLU_023861_4_0_1; -.
DR InParanoid; Q2KJG8; -.
DR OMA; IHHLALH; -.
DR OrthoDB; 1242599at2759; -.
DR TreeFam; TF331303; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000010524; Expressed in laryngeal cartilage and 106 other tissues.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; ISS:HGNC-UCL.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0047323; F:[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; ISS:HGNC-UCL.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:HGNC-UCL.
DR GO; GO:0004740; F:pyruvate dehydrogenase (acetyl-transferring) kinase activity; IBA:GO_Central.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; ISS:HGNC-UCL.
DR GO; GO:0016310; P:phosphorylation; ISS:HGNC-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IBA:GO_Central.
DR Gene3D; 1.20.140.20; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036784; AK/P_DHK_N_sf.
DR InterPro; IPR018955; BCDHK/PDK_N.
DR InterPro; IPR039028; BCKD/PDK.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR11947; PTHR11947; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF69012; SSF69012; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Kinase; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 31..412
FT /note="[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]]
FT kinase, mitochondrial"
FT /id="PRO_0000245575"
FT DOMAIN 159..404
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00972"
FT MOD_RES 52
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 192
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14874"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14874"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55028"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00972"
SQ SEQUENCE 412 AA; 46438 MW; 1E29953147B50ACE CRC64;
MILASVLGSG PRGGPPLRPL LGPALSLRAR STSATDTHHV EMARERSKTV TSFYNQSAID
VAAEKPSVRL TPTMMLYSGR SQDGSHLLKS ARYLQQELPV RIAHRIKGFR SLPFIIGCNP
TILHVHELYI RAFQKLTDFP PIKDQADEAR YCQLVRQLLD DHKDVVTLLA EGLRESRKYI
EDEKLVRYFL DKTLTSRLGI RMLATHHLAL HEDKPDFVGI ICTRLSPKKI IEKWVDFARR
LCEHKYGNAP RVRINGHVAA RFPFIPMPLD YILPELLKNA MRATMESHLD TPYNVPDVVI
TIANNDIDLV IRISDRGGGI AHKDLDRVMD YHFTTAEAST QDPRISPLFG HLDLHSGGQS
GPMHGFGFGL PTSRAYAEYL GGSLRLQSLQ GIGTDVYLRL RHIDGREESF RI
