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Database: UniProt
Entry: X0LV90_FUSOX
LinkDB: X0LV90_FUSOX
Original site: X0LV90_FUSOX 
ID   X0LV90_FUSOX            Unreviewed;       416 AA.
AC   X0LV90;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE            EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN   ORFNames=FOTG_08104 {ECO:0000313|EMBL:EXM25142.1};
OS   Fusarium oxysporum f. sp. vasinfectum 25433.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089449 {ECO:0000313|EMBL:EXM25142.1};
RN   [1] {ECO:0000313|EMBL:EXM25142.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=25433 {ECO:0000313|EMBL:EXM25142.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum Cotton.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXM25142.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=25433 {ECO:0000313|EMBL:EXM25142.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Annotation of Fusarium oxysporum Cotton.";
RL   Submitted (MAY-2012) 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; JH657934; EXM25142.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0LV90; -.
DR   Proteomes; UP000030701; Unassembled WGS sequence.
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   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   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}; Pyruvate {ECO:0000313|EMBL:EXM25142.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT   DOMAIN          24..253
FT                   /note="Branched-chain alpha-ketoacid dehydrogenase
FT                   kinase/Pyruvate dehydrogenase kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10436"
FT   DOMAIN          300..415
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF02518"
SQ   SEQUENCE   416 AA;  47247 MW;  C6AD1062A5A3FD28 CRC64;
     MSWKASERLM DTIRHYARFP ATGVSLRQMV QFGEKPSVGT LFRASQFLAE ELPIRLAHRV
     QELDELPDGL NEMPSVIKVK DWYAQSFEEI TQLPRPQLPS DIRNRLMKPS KAIGRNAFRL
     PAATPNPSID EGEADGWGGL QNDNGKAKAS ARRYFAIVDD SSDWPADLHL YNQRFAQTLH
     HIKRRHDGVV TTMAQGILEY KRRRQRMQID STIQSFLDRF YMSRIGIRML IGQHIALTDQ
     SHHRDPTYVG IICTKTNVQD LAQEAIENAR FVCEDHYGLF EAPKVQLVCN PNLNFMYVPG
     HLSHMLFETL KNSLRAVVET HGMEKQAFPV TKVIVAEGKE DITIKISDEG GGIPRSAIPL
     VWTYMYTTVD RTPSLDPDFD KSDFKAPMAG FGYGLPISRL YARYFGGDLK LISMEG
//
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