UniProt: B8CDF6

Database: UniProt
Entry: B8CDF6_THAPS

LinkDB:  B8CDF6_THAPS 
Original site:  B8CDF6_THAPS

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Ontology (6)   
   GO (6)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
Literature (2)   
   PubMed (2)   
All databases (23)   

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ID   B8CDF6_THAPS            Unreviewed;       338 AA.
AC   B8CDF6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE            EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN   ORFNames=THAPSDRAFT_37571 {ECO:0000313|EMBL:EED88449.1};
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128 {ECO:0000313|EMBL:EED88449.1, ECO:0000313|Proteomes:UP000001449};
RN   [1] {ECO:0000313|EMBL:EED88449.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED88449.1};
RX   PubMed=15459382; DOI=10.1126/science.1101156;
RA   Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA   Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA   Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA   Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA   Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA   Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA   Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA   Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA   Wilkerson F.P., Rokhsar D.S.;
RT   "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT   metabolism.";
RL   Science 306:79-86(2004).
RN   [2] {ECO:0000313|EMBL:EED88449.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED88449.1};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA   Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA   Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA   Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA   Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA   Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA   La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA   Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA   Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA   Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA   Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA   Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA   Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
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; CM000650; EED88449.1; -; Genomic_DNA.
DR   RefSeq; XP_002294094.1; XM_002294058.1.
DR   AlphaFoldDB; B8CDF6; -.
DR   STRING; 35128.B8CDF6; -.
DR   PaxDb; 35128-Thaps37571; -.
DR   EnsemblProtists; EED88449; EED88449; THAPSDRAFT_37571.
DR   GeneID; 7449493; -.
DR   KEGG; tps:THAPSDRAFT_37571; -.
DR   eggNOG; KOG0787; Eukaryota.
DR   HOGENOM; CLU_023861_5_0_1; -.
DR   InParanoid; B8CDF6; -.
DR   OMA; NEMPSIC; -.
DR   Proteomes; UP000001449; Chromosome 15.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004740; F:pyruvate dehydrogenase (acetyl-transferring) kinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; IBA:GO_Central.
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:EED88449.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001449};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT   DOMAIN          195..330
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EED88449.1"
SQ   SEQUENCE   338 AA;  38564 MW;  C37589CFC6771D6F CRC64;
     SEATPLVLLQ VASFLRRELP IRLAHRIQDL SRVPLLQDMK SVQQVKELYT TSFLEIMSVD
     KHPPTREGQE EWEEHFAKIL ENIYERHSSV LVQMARGAFE LRRDAVEFEL MESTHAFLDR
     FYISRIGIRV LIGQYLSLRQ PPVENYVGII CSKTSPYEIV KRAIDDAAFM CTRKYGDAPE
     VIITGRLDMT FPYVPTHLHY IMLELLKNSM RATVEYHGVD ADYPPIKVVI ADGKDNEDVI
     IKVSDEGGGI PRSNMKRIWS YLFTTADPEI QEGMVAFNEN VDHSIDSPLA GLGYGLPISR
     SYTRYFGGDL SIMSMEGYGT DCFVYLTRLG NTREPLPI
//

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