ID XKS1_ASPFU Reviewed; 573 AA. AC Q4WUV8; DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=Probable D-xylulose kinase A; DE Short=Xylulokinase A; DE EC=2.7.1.17; GN Name=xkiA; ORFNames=AFUA_5G09840; OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / OS Af293) (Neosartorya fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=330879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L., RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., RA Barrell B.G., Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(2005). 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}. 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; AAHF01000003; EAL91618.1; -; Genomic_DNA. DR RefSeq; XP_753656.1; XM_748563.1. DR AlphaFoldDB; Q4WUV8; -. DR SMR; Q4WUV8; -. DR STRING; 330879.Q4WUV8; -. DR EnsemblFungi; EAL91618; EAL91618; AFUA_5G09840. DR GeneID; 3511272; -. DR KEGG; afm:AFUA_5G09840; -. DR VEuPathDB; FungiDB:Afu5g09840; -. DR eggNOG; KOG2531; Eukaryota. DR HOGENOM; CLU_016149_5_0_1; -. DR InParanoid; Q4WUV8; -. DR OMA; STHFFNH; -. DR OrthoDB; 1704034at2759; -. DR Proteomes; UP000002530; Chromosome 5. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004856; F:xylulokinase activity; IBA:GO_Central. DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR GO; GO:0005997; P:xylulose metabolic process; IBA:GO_Central. 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 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_0000393519" 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 //