ID   F9XAN5_ZYMTI            Unreviewed;       510 AA.
AC   F9XAN5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   Name=GLK1 {ECO:0000313|EMBL:EGP87741.1};
GN   ORFNames=MYCGRDRAFT_71733 {ECO:0000313|EMBL:EGP87741.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP87741.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP87741.1, 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., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004888}.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}.
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DR   EMBL; CM001200; EGP87741.1; -; Genomic_DNA.
DR   RefSeq; XP_003852765.1; XM_003852717.1.
DR   AlphaFoldDB; F9XAN5; -.
DR   STRING; 336722.F9XAN5; -.
DR   EnsemblFungi; Mycgr3T71733; Mycgr3P71733; Mycgr3G71733.
DR   GeneID; 13397087; -.
DR   KEGG; ztr:MYCGRDRAFT_71733; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   HOGENOM; CLU_014393_5_0_1; -.
DR   InParanoid; F9XAN5; -.
DR   OMA; YPNFEGY; -.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000008062; Chromosome 5.
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:0019660; P:glycolytic fermentation; IEA:EnsemblFungi.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443:SF30; GLUCOKINASE-1-RELATED; 1.
DR   PANTHER; PTHR19443; HEXOKINASE; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU362007};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362007};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362007};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT   DOMAIN          7..215
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          225..502
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   510 AA;  54857 MW;  2354656A8937AAD3 CRC64;
     MALQQAAERV AAEFEYSASD VNRGVTEFIR EMDEGLGKSG ATMSQIPTYV TAVPNGTEKG
     LYMAVDLGGT NFRVCSIQLH GNSTFSLTQS KVAIPKELMV AKTSRELFAF LAKQIEAFLK
     EHHEEHYESH KEKRKGGGDI EQDIFSLGFT FSFPVQQFGI NKGTLIRWTK GFDIPDAIGK
     DVCALLQDEI DRLGLPVRVA ALVNDTVGTL MARSYTSPGK TGTLLGAIFG TGTNGAYVEK
     LSKVTKLDAS AAEVDDSTGE MIINTEWGSF DNHLSVLPQT PYDKALDAES VNPGIQMFEK
     RVSGMFLGEI LRRALLALLK DPAVPLFTDE NSNQNDVHST TNVAADSPLY KQWGLDSSFL
     SIATGDTSAG LKVTRQTLDK DYGVSAASAE DAEAVRLIAA AVGKRAARLS AVAIAAIVIA
     TDKLSKPTDI ATDNDANLEV NEDDIVDVGV DGSLVEFYPR FEEYIREALR EVEKIGKTGE
     RKVRIGIAKD GSGVGAALIA LVADGKGRGE
//