ID   XKS1_ASPOR              Reviewed;         572 AA.
AC   Q2U3V4;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Probable D-xylulose kinase A;
DE            Short=Xylulokinase A;
DE            EC=2.7.1.17;
GN   Name=xkiA; ORFNames=AO090020000603;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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; AP007167; BAE63761.1; -; Genomic_DNA.
DR   RefSeq; XP_001824894.1; XM_001824842.2.
DR   AlphaFoldDB; Q2U3V4; -.
DR   SMR; Q2U3V4; -.
DR   STRING; 510516.Q2U3V4; -.
DR   EnsemblFungi; BAE63761; BAE63761; AO090020000603.
DR   GeneID; 5997088; -.
DR   KEGG; aor:AO090020000603; -.
DR   VEuPathDB; FungiDB:AO090020000603; -.
DR   HOGENOM; CLU_016149_5_0_1; -.
DR   OMA; QHGTVFW; -.
DR   Proteomes; UP000006564; Chromosome 6.
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..572
FT                   /note="Probable D-xylulose kinase A"
FT                   /id="PRO_0000393522"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         365
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         470..471
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         474
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   572 AA;  62926 MW;  3A2C8A5EEA3E92D9 CRC64;
     MQGPLYIGFD LSTQQLKALV VNSDLKVVYV SKFDFDADSR GFPIKKGVIT NEAEHEVYAP
     VALWLQALDG VLEGLKKQGL DFARVKGISG AGQQHGSVYW GQDAERLLKE LDSGKSLEDQ
     LSGAFSHPYS PNWQDSSTQK ECDEFDAFLG GADKLANATG SKAHHRFTGP QILRFQRKYP
     EVYKKTSRIS LVSSFLASLF LGHIAPLDTS DVCGMNLWNI KQGAYDEKLL QLCAGPSGVE
     DLKRKLGAVP EDGGINLGQI DRYYIERYGF SSDCTIIPAT GDNPATILAL PLRPSDAMVS
     LGTSTTFLMS TPNYMPDPAT HFFNHPTTAG LYMFMLCYKN GGLAREHIRD AINDKLGMAG
     DKDPWANFDK ITLETAPMGQ KKDSDPMKMG LFFPRPEIVP NLRAGQWRFD YNPADGSLHE
     TNGGWNKPAD EARAIVESQF LSLRLRSRGL TASPGQGMPA QPRRVYLVGG GSKNKAIAKV
     AGEILGGSDG VYKLEIGDNA CALGAAYKAV WALERKDGQT FEDLIGQRWR EEDFIEKIAD
     GYQKGVFEKY GAALEGFEKM ELQVLKQEGE TR