ID F9WZ98_ZYMTI Unreviewed; 593 AA.
AC F9WZ98;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN Name=MgXKS1 {ECO:0000313|EMBL:EGP91268.1};
GN ORFNames=MYCGRDRAFT_53056 {ECO:0000313|EMBL:EGP91268.1};
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:EGP91268.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP91268.1, 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 -!- FUNCTION: Highly specific D-xylulose kinase which participates in the
CC catabolism of xylose. Xylose is a major component of hemicelluloses
CC such as xylan. Most fungi utilize D-xylose via three enzymatic
CC reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and
CC xylulokinase, to form xylulose 5-phosphate, which enters pentose
CC phosphate pathway. {ECO:0000256|ARBA:ARBA00025184,
CC ECO:0000256|RuleBase:RU367058}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:10964, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57737, ChEBI:CHEBI:456216;
CC EC=2.7.1.17; Evidence={ECO:0000256|ARBA:ARBA00001811,
CC ECO:0000256|RuleBase:RU367058};
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|RuleBase:RU367058}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001196; EGP91268.1; -; Genomic_DNA.
DR RefSeq; XP_003856292.1; XM_003856244.1.
DR AlphaFoldDB; F9WZ98; -.
DR STRING; 336722.F9WZ98; -.
DR EnsemblFungi; Mycgr3T53056; Mycgr3P53056; Mycgr3G53056.
DR GeneID; 13394773; -.
DR KEGG; ztr:MYCGRDRAFT_53056; -.
DR eggNOG; KOG2531; Eukaryota.
DR HOGENOM; CLU_016149_5_0_1; -.
DR InParanoid; F9WZ98; -.
DR OMA; STHFFNH; -.
DR OrthoDB; 1704034at2759; -.
DR Proteomes; UP000008062; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07776; FGGY_D-XK_euk; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042024; D-XK_euk.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR PANTHER; PTHR10196; SUGAR KINASE; 1.
DR PANTHER; PTHR10196:SF57; XYLULOSE KINASE; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU367058};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU367058};
KW Kinase {ECO:0000256|RuleBase:RU367058, ECO:0000313|EMBL:EGP91268.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367058};
KW Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW Transferase {ECO:0000256|RuleBase:RU367058};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629,
KW ECO:0000256|RuleBase:RU367058}.
FT DOMAIN 144..300
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 309..520
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 593 AA; 64633 MW; B32106A62ED882DD CRC64;
MAGSGSLYLG FDLSTQQLKG LVVSSDLKLI HEAKVDFDQD LGKKYGIEKG VLTNPSEGEV
FAPPAMWLEA LDLVLDRLKE AGLDFGRVKG VSGAGMQHGT VFWSRHAESL LANLDAGQPL
VGQLDAEVES GRRGAFAHPM SPNWQDASTQ EQCDAFDVEL EDKETLANVT GSKAHHRFSG
PQIMRYRKKH AEHYEQTARI SLVSSFLASI LLGNIAPIDI SDVTGTNLWN LDKAAWDRKL
VALAAGGEDK ADELLTKLGD VTIDGGKTFG TISNYFVNRY GFAQDCNIIP FTGDNPATIL
ALPLRAGDAM VSLGTSTTFL MSTSQYKPDP AYHFMNHPTT PGLYMFMLCY KNGGLAREQI
RDQLDPSGKW DHFDSTALST APVSQKSDGE PMRIGLYFPR PEIVPNLPSG QWRFNYNPST
DSLDEVSSDF LPDDARNIIE SQMLSLRLRS HNLVHPGKDP KSGETLPAQP RRVYLVGGGS
ANPAIAKICG EVLGGVEGVF KLDIGGNACA LGAAYKAVWG CERKGGESFE DLIGKRWDEA
SFVKRVADGY TKGVFEKYGE AVKGFEKMEQ VVLKKEVELL GQRGGGLMYP PNK
//
