ID B2G4U8_ZYGRO Unreviewed; 498 AA.
AC B2G4U8;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN Name=Zr_KLLA0F27423g {ECO:0000313|EMBL:CAQ43607.1};
GN ORFNames=Zrou_10p43 {ECO:0000313|EMBL:CAQ43607.1};
OS Zygosaccharomyces rouxii (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=4956 {ECO:0000313|EMBL:CAQ43607.1};
RN [1] {ECO:0000313|EMBL:CAQ43607.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 732 {ECO:0000313|EMBL:CAQ43607.1};
RA Gordon J.L., Wolfe K.H.;
RT "Zygosaccharomyces rouxii homologs of Saccharomyces cerevisiae chromosome
RT III.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; AM989989; CAQ43607.1; -; Genomic_DNA.
DR RefSeq; XP_002496783.1; XM_002496738.1.
DR AlphaFoldDB; B2G4U8; -.
DR GeneID; 8204039; -.
DR KEGG; zro:ZYRO0D08052g; -.
DR OMA; TIKHYSN; -.
DR OrthoDB; 3058550at2759; -.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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 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 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.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT DOMAIN 343..491
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 498 AA; 56524 MW; F43E702F497DBC0A CRC64;
MTKIKFNSGL LKQIWNYSEL PQTGISLRQM CQFGANPNPA TLFKASCFVL RELPIRLAHR
IKELESLPNG LNKMNDVIQV RDWYTQSFKE LYEFAHDRST SNGKLYQMLY GGLEPDTPME
SEVLRNIIQL CYRDEELDSK HGRSNTSVPH RNTFVDDGLV VTKRKWSVSN QSLSSSRGQV
LTPKKYYSSP LVTSLEVWPK EILKFNAALF KVLHNIKVRH NATVVTLAKG VLKWKKTCQQ
NMFDDSVQSF LDRFYMSRIG IRMLIAQHLD LLEPSLHCQN GKSDSYVGSI CTKTNITQIA
EDAIDNAKLI CSEHYGLFEA PEVELLCFPK NATGLNNEIE FMYVPGHLIH MLVETLKNAL
RATVEKTVES NPGMDVYDLK FPHVKVIICE GLEDITVKIS DEGGGIARSN LPLIWTYLYS
TMPDDCQLEL MKDECDENPR VSSFVNNVPL AGYGYGLALS RLYARYFGGD LKLISMEGFG
TDVYLHLNRL STSSEPLQ
//