ID   XKS1_ARTOC              Reviewed;         570 AA.
AC   C5FSW4;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Probable D-xylulose kinase A;
DE            Short=Xylulokinase A;
DE            EC=2.7.1.17;
GN   Name=xkiA; ORFNames=MCYG_05786;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS995705; EEQ32967.1; -; Genomic_DNA.
DR   RefSeq; XP_002845917.1; XM_002845871.1.
DR   AlphaFoldDB; C5FSW4; -.
DR   SMR; C5FSW4; -.
DR   STRING; 554155.C5FSW4; -.
DR   GeneID; 9224217; -.
DR   VEuPathDB; FungiDB:MCYG_05786; -.
DR   eggNOG; KOG2531; Eukaryota.
DR   HOGENOM; CLU_016149_5_0_1; -.
DR   OMA; STHFFNH; -.
DR   OrthoDB; 1704034at2759; -.
DR   Proteomes; UP000002035; 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   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   PANTHER; PTHR10196; SUGAR KINASE; 1.
DR   PANTHER; PTHR10196:SF57; XYLULOSE KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 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..570
FT                   /note="Probable D-xylulose kinase A"
FT                   /id="PRO_0000393525"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         363
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   570 AA;  62891 MW;  30B542C940D3778D CRC64;
     MGSSGGPLYI GFDLSTQQLK GLVVSSDLKV VHIAKFDFDS DSKGFNISKG VLTNEDEGEV
     FAPVAMWLQA LDAVLQDLKH QGLDFSLVRG ISGAGQQHGS VYWNESAEEI LGGLDGGKTL
     EDQLQQALSY PYSPNWQDSS TQRECDEFDA FLGSEEELAR VTGSKAHHIL RFQRKHPDAY
     RKTSRISLVS SFLASIFLGS VAPFDISDVC GMNLWDMPMN RWNERLLKLC AGEAGPEELK
     KKLGDVPHDG GQELGKISSY FAKRYSFHPD CAITPSTGDN PATILALPLR PLDAMVSLGT
     STTFLMSTPQ YKPDPSTHFF NHPTTPGLYM FMLCYKNGGL AREQVRDAIN ATSGEKTDPS
     NPWSNFDRVL LETPPGGQKA GSGPMKMGLF FPRPEIVPNL GEGEWHFNYT PGQANEELKE
     TDEGWTHPRD DARAIVESQF LSLRLRSKEL VHSPSGGVPP QPRRIYLVGG GSRNAAIAKV
     AGEVLGGIEG VYKLDVGENA CALGAAYKAV WALERAPDQT FEDLIGRRWR EDEFVEKIAD
     GFQPDIFEKY RQAVQGFEKM EKQVLMEAKQ
//