ID   XKS1_SCHPO              Reviewed;         555 AA.
AC   Q9C0U6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Xylulose kinase;
DE            Short=Xylulokinase;
DE            EC=2.7.1.17;
GN   Name=xks1 {ECO:0000250|UniProtKB:P42826}; ORFNames=SPCPJ732.02c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1] {ECO:0000312|EMBL:CAC34988.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2] {ECO:0000305}
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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; Evidence={ECO:0000250|UniProtKB:P42826};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255}.
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DR   EMBL; CU329672; CAC34988.1; -; Genomic_DNA.
DR   RefSeq; NP_587930.1; NM_001022921.2.
DR   AlphaFoldDB; Q9C0U6; -.
DR   SMR; Q9C0U6; -.
DR   BioGRID; 276004; 22.
DR   STRING; 284812.Q9C0U6; -.
DR   MaxQB; Q9C0U6; -.
DR   PaxDb; 4896-SPCPJ732-02c-1; -.
DR   EnsemblFungi; SPCPJ732.02c.1; SPCPJ732.02c.1:pep; SPCPJ732.02c.
DR   PomBase; SPCPJ732.02c; xks1.
DR   VEuPathDB; FungiDB:SPCPJ732.02c; -.
DR   eggNOG; KOG2531; Eukaryota.
DR   HOGENOM; CLU_016149_5_0_1; -.
DR   InParanoid; Q9C0U6; -.
DR   OMA; STHFFNH; -.
DR   PhylomeDB; Q9C0U6; -.
DR   Reactome; R-SPO-5661270; Formation of xylulose-5-phosphate.
DR   PRO; PR:Q9C0U6; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004856; F:xylulokinase activity; ISO:PomBase.
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; ISO:PomBase.
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   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase; Xylose metabolism.
FT   CHAIN           1..555
FT                   /note="Xylulose kinase"
FT                   /id="PRO_0000311717"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         357
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         455..456
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         459
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   555 AA;  61683 MW;  610CE6A309244E01 CRC64;
     MFLGLDLSTQ QLKGVVIDES LNVHQEVAVD FDRDLSDYNT IKGVYRNGYE VFAPVCMWLD
     AIDLLFERLK ASVDVSKIQA ISGAGQQHAS VFLLKGSKKA LNSLDAKSSL KQQLESLIHP
     TSPNWQDAST TKECEELESC IGGAKALADL TGSKAHLRFT GPQIKRFRRL HPETYENTER
     IALVSNFLAS VLLQTEAPLD ISDVCGMNLW DIQNEKFDIR LLEEVAGNSK GPDLANKLGT
     VEINGAKHLG PIGKYFVKKY GFSPNCQIIP LTGDNPATIL SLPLRPGKDV LLSLGTSTTA
     LMATQNYVCS PEYHMFAHPV TQNHYMVMLC YKNGSLAREQ VRNTINEKYN VSDNTSWDRF
     NESILNPNIK GAGEKKQLGL FYPQREILPA VGPGTWRFAI QGTELYQVDK DEESWDYPDE
     DASAIVESQN LDIRMRITPL LTGIPQPDRV YVVGGASRNE AIVFKISQVL GCDVYRLKHG
     GSNACAVGGA IKAAYAMNGK GFTFEEYVNK SWDESKKIEL IMNKPSAQTY EEYGKLLPFL
     KKAEDIAIQQ SDIRH
//