ID C4QWE7_KOMPG Unreviewed; 454 AA.
AC C4QWE7;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN OrderedLocusNames=PAS_chr1-1_0202 {ECO:0000313|EMBL:CAY67570.1};
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY67570.1, ECO:0000313|Proteomes:UP000000314};
RN [1] {ECO:0000313|EMBL:CAY67570.1, ECO:0000313|Proteomes:UP000000314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
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 Evidence={ECO:0000256|ARBA:ARBA00036431};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU366032}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000256|ARBA:ARBA00006155, ECO:0000256|RuleBase:RU366032}.
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DR EMBL; FN392319; CAY67570.1; -; Genomic_DNA.
DR RefSeq; XP_002489851.1; XM_002489806.1.
DR AlphaFoldDB; C4QWE7; -.
DR SMR; C4QWE7; -.
DR STRING; 644223.C4QWE7; -.
DR EnsemblFungi; CAY67570; CAY67570; PAS_chr1-1_0202.
DR GeneID; 8197923; -.
DR KEGG; ppa:PAS_chr1-1_0202; -.
DR eggNOG; KOG0787; Eukaryota.
DR HOGENOM; CLU_023861_5_1_1; -.
DR InParanoid; C4QWE7; -.
DR OMA; NEMPSIC; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000000314; Chromosome 1.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004740; F:pyruvate dehydrogenase (acetyl-transferring) kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16929; HATPase_PDK-like; 1.
DR Gene3D; 1.20.140.20; Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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:SF3; [PYRUVATE DEHYDROGENASE (ACETYL-TRANSFERRING)] KINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11947; PYRUVATE DEHYDROGENASE KINASE; 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; SSF69012; alpha-ketoacid dehydrogenase kinase, N-terminal domain; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU366032};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU366032};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU366032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366032};
KW Reference proteome {ECO:0000313|Proteomes:UP000000314};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 312..447
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 454 AA; 51663 MW; 591A9417156D225D CRC64;
MSWKLTNQLR DKIYRYARFP PTGVSLRQMV QFGPKPSAGT LFHASQFVVE ELPIRLAHRV
KELEELPDDL NQMPSIQRVR DWYARSFDEL TSLAAPDISD ELRNLLYEDG HNHLYQPEMN
EMPPNNIQVQ HSDTSFDDDG LVISNRHHHS KATSASQNQS SNKKKYYLSC PSNVVYPKEV
YEYNKLVADT LKTIKKRHDA TVPTVARGVQ EWKHAKNQMS IESNIQSFLD RFYLSRIGIR
ILIGQTIALN QDIGNDNYVG IICLNTNVAD VARDAIDSAR FTCEEHYGLF EAPKVQLYCP
EDLTFMYVPG HLIHMLFETL KNSLRATVEH HIQLNPGVDI EDIEFPPVKI IVAEGNEDIT
IKISDEGGGI PRSAISLIWT YLYTTVEEMP SLDHDTDAKA DFRAPMSGLG FGLPLSRLYA
RYFGGDLKLI SMENYGTDVY LHLNRLSSSS EPLP
//
