XKS1_ASPFU
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 03-AUG-2022, entry version 87.
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 Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
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 / Af293 / CBS 101355 / FGSC A1100;
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}.
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DR EMBL; AAHF01000003; EAL91618.1; -; Genomic_DNA.
DR RefSeq; XP_753656.1; XM_748563.1.
DR AlphaFoldDB; Q4WUV8; -.
DR SMR; Q4WUV8; -.
DR STRING; 746128.CADAFUBP00005619; -.
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; QHGTVFW; -.
DR OrthoDB; 592116at2759; -.
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:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
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:0005998; P:xylulose catabolic process; IEA:EnsemblFungi.
DR GO; GO:0005997; P:xylulose metabolic process; IBA:GO_Central.
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_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
