ID H8X4M8_CANO9 Unreviewed; 523 AA.
AC H8X4M8;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN ORFNames=CORT_0D01220 {ECO:0000313|EMBL:CCG22970.1};
OS Candida orthopsilosis (strain 90-125) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG22970.1, ECO:0000313|Proteomes:UP000005018};
RN [1] {ECO:0000313|EMBL:CCG22970.1, ECO:0000313|Proteomes:UP000005018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT "Sequence and analysis of the genome of the pathogenic yeast Candida
RT orthopsilosis.";
RL PLoS ONE 7:e35750-e35750(2012).
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; HE681722; CCG22970.1; -; Genomic_DNA.
DR RefSeq; XP_003869107.1; XM_003869058.1.
DR AlphaFoldDB; H8X4M8; -.
DR GeneID; 14540238; -.
DR KEGG; cot:CORT_0D01220; -.
DR eggNOG; KOG0787; Eukaryota.
DR HOGENOM; CLU_023861_5_1_1; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000005018; Chromosome 4.
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}; Pyruvate {ECO:0000313|EMBL:CCG22970.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 369..516
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 523 AA; 59235 MW; CF4C969812728C9A CRC64;
MGTGWELTKA LKEKIFQYAI YNQTPISLRQ MVQFGPTPSP GSIFLASKFI VEELPIRLAK
KVKDLEYAPL GLNESPSTIK VKDWYAQSFQ ELTELPKPKI DENLKKLLYS NNGNSNGFKV
DDLDDQPNIQ KEVHKISEVQ EDNPAINNIF SDDGIVVRHH HHHQNSDQTK SPTITKTRIP
SKDQENTTIR SESPTYGMTY FSPCPTNIVW PKEVYAYNKL VFETLEKIKK RHDATVATMA
QGVQEWKAKN KTVFVNSQIQ TFLDRFYMSR IGIRMLIGQH LALNMAQNSP TKQRLSKLIN
GSEGSTKKPG RSNYVGVICT DCNVGEIAED AIETAKYICE EFYGLFEAPE IQLVAPQQDI
NFMYVPGHLI HMLFETLKNS LRATIEFHTP KLKQKYVEEN PGTKLDEVDI NDLEYPPIKV
IISEGTEDIA IKISDEGGGI PRSSLPLIWT YLYTTVDETP KLEPEYSQTS FKAPMAGFGY
GLPISRLYAQ YFGGDLKLIS MEGYGTDVYL HLNRLSSSNE PLP
//
