ID   XKS1_EMENI              Reviewed;         581 AA.
AC   Q5ASE0; C8V9P8;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-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=AN8790;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000161; EAA60583.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF78014.1; -; Genomic_DNA.
DR   RefSeq; XP_682059.1; XM_676967.1.
DR   AlphaFoldDB; Q5ASE0; -.
DR   SMR; Q5ASE0; -.
DR   STRING; 162425.CADANIAP00006272; -.
DR   EnsemblFungi; CBF78014; CBF78014; ANIA_08790.
DR   EnsemblFungi; EAA60583; EAA60583; AN8790.2.
DR   GeneID; 2868421; -.
DR   KEGG; ani:AN8790.2; -.
DR   VEuPathDB; FungiDB:AN8790; -.
DR   eggNOG; KOG2531; Eukaryota.
DR   HOGENOM; CLU_016149_5_0_1; -.
DR   InParanoid; Q5ASE0; -.
DR   OMA; QHGTVFW; -.
DR   OrthoDB; 592116at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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..581
FT                   /note="Probable D-xylulose kinase A"
FT                   /id="PRO_0000393524"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         291
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         373
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         480..481
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         484
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   581 AA;  64025 MW;  551C8D374CDEF3D9 CRC64;
     MSSRSSSPLK GPLYIGFDLS TQQLKGLVVN SDLKVVYSSI FDFDADSQGF PIKKGVLTNE
     AEHEVFAPVA LWLQALDSVL DGLKKQGLDF SHVRGISGAG QQHGSVYWGQ DAEKLLNGLD
     AGKRLQEQLE GAFSHPYSPN WQDSSTQKEC DEFDEYLGGA DKLAEATGSK AHHRFTGPQI
     LRFQKKYPDV YKKTSRISLV SSFLASLFLG HIAPLDISDV CGMNLWNIHK GAYDEDLLKL
     CAGPHGVEDL KRKLGDVPED GGIDLGKVHR YYVDRYGFSP ECTVIPSTGD NPATILALPL
     RPSDAMVSLG TSTTFLMSTP SYKADPATHF FNHPTTPGLY MFMLCYKNGG LAREKIRDAI
     NDAKNEKNPS NPWANFDSVA LQTPPLGQTS PSDPMKMGLF FPRPEIVPNL RAGQWLFNYD
     PSTGNLTETL NGEGWNRPAD EARAIIESQM LSLRLRSRGL TSSPGGDIPA QPRRVYLVGG
     GSKNKTIAKI AGEILGGSEG VYKLEIGDNA CALGAAYKAV WALERKKDQT FEDLIGARWH
     EEEFIEKIAD GYQKEAFERY GKAVEGFEKM EQRVLEQEGR K