ID   XKS1_NEOFI              Reviewed;         573 AA.
AC   A1DEK3;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Probable D-xylulose kinase A;
DE            Short=Xylulokinase A;
DE            EC=2.7.1.17;
GN   Name=xkiA; ORFNames=NFIA_077470;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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; DS027696; EAW17810.1; -; Genomic_DNA.
DR   RefSeq; XP_001259707.1; XM_001259706.1.
DR   AlphaFoldDB; A1DEK3; -.
DR   SMR; A1DEK3; -.
DR   STRING; 36630.CADNFIAP00007712; -.
DR   PRIDE; A1DEK3; -.
DR   EnsemblFungi; EAW17810; EAW17810; NFIA_077470.
DR   GeneID; 4586369; -.
DR   KEGG; nfi:NFIA_077470; -.
DR   VEuPathDB; FungiDB:NFIA_077470; -.
DR   eggNOG; KOG2531; Eukaryota.
DR   HOGENOM; CLU_016149_5_0_1; -.
DR   OMA; QHGTVFW; -.
DR   OrthoDB; 592116at2759; -.
DR   Proteomes; UP000006702; 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; Reference proteome; Transferase; Xylose metabolism.
FT   CHAIN           1..573
FT                   /note="Probable D-xylulose kinase A"
FT                   /id="PRO_0000393526"
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;  63054 MW;  487BF898987F5640 CRC64;
     MTSQGPLYIG FDLSTQQLKG LVVNSELKVV HVSKFDFDAD SHGFSIKKGV LTNEAEHEVF
     APVALWLQAL DGVLDGLRKQ GLDFSRVKGI SGAGQQHGSV YWGENAESLL KSLDSSKSLE
     EQLSGAFSHP FSPNWQDAST QKECDEFDAF LGGPEQLAEA TGSKAHHRFT GPQILRMQRK
     YPEVYRKTAR ISLVSSFLAS LLLGYIAPMD ISDVCGMNLW DIKKGAYNEK LLGLCAGPFG
     AEDLKRKLGD VPEDGGLRLG KINRYFVERY GFSSNCEILP STGDNPATIL ALPLRPSDAM
     VSLGTSTTFL MSTPSYKPDP ATHFFNHPTT PGLYMFMLCY KNGGLAREHV RDAINEKSGS
     GASQSWESFD KIMLETPPMG QKTESGPMKM GLFFPRPEIV PNVRSGQWRF TYDPASDTLT
     ETEDGWNKPS DEARAIVESQ MLSLRLRSRG LTQSPGDGLP PQPRRVYLVG GGSKNKAIAK
     VAGEILGGSD GVYKLDVGDN ACALGAAYKA VWAIERKPGQ TFEDLIGQRW REEEFIEKIA
     DGYQKGVFEK YGKAVEGFER MEQQVLKQEA ARK