ID   PDK_ASCSU               Reviewed;         399 AA.
AC   O02623;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=[Pyruvate dehydrogenase (acetyl-transferring)] kinase, mitochondrial;
DE            Short=Pyruvate dehydrogenase kinase;
DE            EC=2.7.11.2;
DE   Flags: Precursor;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9578613; DOI=10.1006/abbi.1998.0627;
RA   Chen W., Huang X., Komuniecki P.R., Komuniecki R.;
RT   "Molecular cloning, functional expression, and characterization of pyruvate
RT   dehydrogenase kinase from anaerobic muscle of the parasitic nematode
RT   Ascaris suum.";
RL   Arch. Biochem. Biophys. 353:181-189(1998).
CC   -!- FUNCTION: Inhibits the mitochondrial pyruvate dehydrogenase complex by
CC       phosphorylation of the E1 alpha subunit, thus contributing to the
CC       regulation of glucose metabolism.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP
CC         + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit];
CC         Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.2;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC       {ECO:0000305}.
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DR   EMBL; U94519; AAB52573.1; -; mRNA.
DR   AlphaFoldDB; O02623; -.
DR   SMR; O02623; -.
DR   BioCyc; MetaCyc:MON-18304; -.
DR   BRENDA; 2.7.11.2; 474.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004740; F:pyruvate dehydrogenase (acetyl-transferring) kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   PANTHER; PTHR11947; PTHR11947; 1.
DR   Pfam; PF10436; BCDHK_Adom3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
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   ATP-binding; Carbohydrate metabolism; Glucose metabolism; Kinase;
KW   Mitochondrion; Nucleotide-binding; Transferase; Transit peptide.
FT   TRANSIT         1..18
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..399
FT                   /note="[Pyruvate dehydrogenase (acetyl-transferring)]
FT                   kinase, mitochondrial"
FT                   /id="PRO_0000023449"
FT   DOMAIN          123..360
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   BINDING         247..254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         305..306
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         321..326
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   399 AA;  45402 MW;  31F0EDA7D4F0412A CRC64;
     MFLTRRLLGP FTSAIARKLE HYSQFQPSSL TIQQYLDFGQ TGTMKSSFLF LKNELLVRLA
     NIMQEISLLP PTLLKMPSRR LVSNWYCESF EDLLQFEHAQ VEPDIMSKFN DQLQTILKRH
     SRVVETMAEG LIELRESEGV DIASERGIQY FLDRFYINRI SIRMLQNQHL VVFGVVLPES
     PRHIGCIDPG CDVESVVHDA YENARFLCER YYLTAPGMKL EMHNSVNPGM PISIVAVPSH
     LYHIMFELFK NSMRATVENH GADEDLPPIK VMVVRGAEDL SIKISDRGGG VSRTILDRLF
     TYMYSTAPPP PRDGTQPPLA GYGYGLPLSR LYARYFHGDM YLVSMEGYGT DAMIFLKAIP
     VEASEVLPIY STSSRRQLTM SPQAADWSHQ LPNHGNRNL