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Database: UniProt/TrEMBL
Entry: F9XDZ5_ZYMTI
LinkDB: F9XDZ5_ZYMTI
Original site: F9XDZ5_ZYMTI 
ID   F9XDZ5_ZYMTI            Unreviewed;       496 AA.
AC   F9XDZ5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   07-JUN-2017, entry version 38.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   Name=HKX1 {ECO:0000313|EMBL:EGP86719.1};
GN   ORFNames=MYCGRDRAFT_100586 {ECO:0000313|EMBL:EGP86719.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf
OS   blotch fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP86719.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP86719.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J.,
RA   Crane C.F., Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J.,
RA   Aerts A., Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J.,
RA   van der Burgt A., Canto-Canche B., Churchill A.C.L., Conde-Ferraez L.,
RA   Cools H.J., Coutinho P.M., Csukai M., Dehal P., De Wit P.,
RA   Donzelli B., van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E.,
RA   Henrissat B., Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y.,
RA   Kuzniar A., Lindquist E., Lombard V., Maliepaard C., Martins N.,
RA   Mehrabi R., Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A.,
RA   Schmutz J., Schouten H.J., Shapiro H., Stergiopoulos I.,
RA   Torriani S.F.F., Tu H., de Vries R.P., Waalwijk C., Ware S.B.,
RA   Wiebenga A., Zwiers L.-H., Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella
RT   graminicola reveals dispensome structure, chromosome plasticity, and
RT   stealth pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00672880}.
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DR   EMBL; CM001201; EGP86719.1; -; Genomic_DNA.
DR   RefSeq; XP_003851743.1; XM_003851695.1.
DR   EnsemblFungi; Mycgr3T100586; Mycgr3P100586; Mycgr3G100586.
DR   GeneID; 13401743; -.
DR   KEGG; ztr:MYCGRDRAFT_100586; -.
DR   InParanoid; F9XDZ5; -.
DR   KO; K00844; -.
DR   OrthoDB; EOG092C2JW4; -.
DR   Proteomes; UP000008062; Chromosome 6.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008865; F:fructokinase activity; IEA:EnsemblFungi.
DR   GO; GO:0004340; F:glucokinase activity; IEA:EnsemblFungi.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0019158; F:mannokinase activity; IEA:EnsemblFungi.
DR   GO; GO:0001678; P:cellular glucose homeostasis; IEA:InterPro.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006000; P:fructose metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:EnsemblFungi.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; PTHR19443; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PROSITE; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672869};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008062};
KW   Glycolysis {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672870};
KW   Kinase {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00672871};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672883};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW   Transferase {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672884}.
FT   DOMAIN       27    221       Hexokinase_1. {ECO:0000259|Pfam:PF00349}.
FT   DOMAIN      227    472       Hexokinase_2. {ECO:0000259|Pfam:PF03727}.
SQ   SEQUENCE   496 AA;  54895 MW;  5FC8E66F2694F97E CRC64;
     MVGLGPRRKP SRKGSMADMP QDLLSEIKRL EELFIVDTPK LKSITEHFIS ELAKGLTKEG
     GSIPMNPTWV MGYPTGHETG TFLALDMGGT NLRVCEINLP EEKGEFDIIQ SKYRMPEELK
     TGNADELWGY IADCLQQFIE YHHEGEKLDK LPLGFTFSYP ATQDFIDHGV LQRWTKGFDI
     DGVEGKDVVP PFEAALQERG VPIKLTALIN DTTGTLIASS YTDPEMKIGC IFGTGCNAAY
     MEHAGEIPKL EDWKMDPKQE IAINCEWGAF DNEHKVLPRT PYDIIIDKDS PRPGQQAFEK
     MIAGLYLGEL FRLVLVDLHE KNVVFQGQDI AALRKPYSLD ASYLSDIEND PFENLQETAD
     NFKSVLNITT SKPELELIRR LAELIGTRSA RLSACGVAAI CKKKGYKTAH VGADGSVFNK
     YPHFKQRGAA ALKEILDWET GRDGKPLGKG NDPVEIMPAE DGSGVGAALI AALTLKRAKE
     GKLEGIRDAE SMLKGM
//
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