PDHK2_CAEEL
ID PDHK2_CAEEL Reviewed; 401 AA.
AC Q02332;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Probable [pyruvate dehydrogenase (acetyl-transferring)] kinase, mitochondrial;
DE Short=Pyruvate dehydrogenase kinase;
DE EC=2.7.11.2;
DE Flags: Precursor;
GN Name=pdhk-2; ORFNames=ZK370.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(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. {ECO:0000250}.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000305}.
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DR EMBL; FO080164; CCD61725.1; -; Genomic_DNA.
DR PIR; S44666; S44666.
DR RefSeq; NP_498928.1; NM_066527.3.
DR AlphaFoldDB; Q02332; -.
DR SMR; Q02332; -.
DR BioGRID; 41429; 9.
DR DIP; DIP-26171N; -.
DR STRING; 6239.ZK370.5; -.
DR EPD; Q02332; -.
DR PaxDb; Q02332; -.
DR PeptideAtlas; Q02332; -.
DR EnsemblMetazoa; ZK370.5.1; ZK370.5.1; WBGene00022719.
DR GeneID; 176226; -.
DR KEGG; cel:CELE_ZK370.5; -.
DR CTD; 176226; -.
DR WormBase; ZK370.5; CE00397; WBGene00022719; pdhk-2.
DR eggNOG; KOG0787; Eukaryota.
DR GeneTree; ENSGT01030000234646; -.
DR HOGENOM; CLU_023861_1_0_1; -.
DR InParanoid; Q02332; -.
DR OMA; APQIGDH; -.
DR OrthoDB; 1242599at2759; -.
DR PhylomeDB; Q02332; -.
DR Reactome; R-CEL-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-CEL-5362517; Signaling by Retinoic Acid.
DR PRO; PR:Q02332; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022719; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004740; F:pyruvate dehydrogenase (acetyl-transferring) kinase activity; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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 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 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Glucose metabolism; Kinase;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..401
FT /note="Probable [pyruvate dehydrogenase (acetyl-
FT transferring)] kinase, mitochondrial"
FT /id="PRO_0000023450"
FT DOMAIN 131..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 401 AA; 45282 MW; 00754E7999BACC12 CRC64;
MRFSRKLLGP FVGSLAKKLD YYSQFQPSSL TIQQYLDFGR IGTSANSYTF LKNELLVRLA
NIMQEFTLLP PKLLQMPSSK MVSNWYAESF EDLLLFEASD SSPEQVARFN DQLTVVLKRH
AHVVETMAEG LIELRESDGV DIASEKGIQY FLDRFYINRI SIRMLQNQHL VVFGNVLPES
PRHVGCIDPA CDVESVVYDA FENARFLCDR YYLTSPSMKL EMHNAVEKGK PISIVAVPSH
LYHMMFELFK NAMRATVEYH GVDDDLPDIK VYVVKGQEDL SIKICDRGGG VSRTILERLY
NYMYSTAPPP PRDGTQAPLA GYGYGLPLSR LYARYFLGDL FLVSMEGHGT DACIYLKAVP
VEASEVLPIY STSSRRNLTM GPQVADWSHH VPGQGNRPAQ S
