ID   XKS1_ASPFC              Reviewed;         573 AA.
AC   B0Y4D5;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Probable D-xylulose kinase A;
DE            Short=Xylulokinase A;
DE            EC=2.7.1.17;
GN   Name=xkiA; ORFNames=AFUB_057400;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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 (By similarity). {ECO:0000250}.
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: By D-xylose, L-arabinose or L-arabitol.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR   EMBL; DS499597; EDP51726.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y4D5; -.
DR   SMR; B0Y4D5; -.
DR   PRIDE; B0Y4D5; -.
DR   EnsemblFungi; EDP51726; EDP51726; AFUB_057400.
DR   VEuPathDB; FungiDB:AFUB_057400; -.
DR   HOGENOM; CLU_016149_5_0_1; -.
DR   PhylomeDB; B0Y4D5; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0005998; P:xylulose catabolic process; IEA:EnsemblFungi.
DR   CDD; cd07776; FGGY_D-XK_euk; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR042024; D-XK_euk.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase;
KW   Nucleotide-binding; Transferase; Xylose metabolism.
FT   CHAIN           1..573
FT                   /note="Probable D-xylulose kinase A"
FT                   /id="PRO_0000393517"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         471..472
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         475
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   573 AA;  62940 MW;  FB1E317F57D2B829 CRC64;
     MTSQGPLYIG FDLSTQQLKG LVVNSELKVV HISKFDFDAD SHGFSIKKGV LTNEAEHEVF
     APVALWLQAL DGVLNGLRKQ GLDFSRVKGI SGAGQQHGSV YWGENAESLL KSLDSSKSLE
     EQLSGAFSHP FSPNWQDAST QKECDEFDAF LGGPEQLAEA TGSKAHHRFT GPQILRMQRK
     YPEVYKKTAR ISLVSSFLAS LLLGHIAPMD ISDVCGMNLW DIKKGAYNEK LLGLCAGPFG
     VEDLKRKLGA VPEDGGLRLG KINRYFVERY GFSSDCEILP STGDNPATIL ALPLRPSDAM
     VSLGTSTTFL MSTPNYKPDP ATHFFNHPTT PGLYMFMLCY KNGGLAREHV RDAINEKSGS
     GASQSWESFD KIMLETPPMG QKTESGPMKM GLFFPRPEIV PNVRSGQWRF TYDPASDALT
     ETEDGWNTPS DEARAIVESQ MLSLRLRSRG LTQSPGDGLP PQPRRVYLVG GGSKNKAIAK
     VAGEILGGSD GVYKLDVGDN ACALGAAYKA VWAIERKPGQ TFEDLIGQRW REEEFIEKIA
     DGYQKGVFEK YGKAVEGFEK MEQQVLKQEA ARK