XKS1_SCHPO
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 03-AUG-2022, entry version 108.
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; 4896.SPCPJ732.02c.1; -.
DR MaxQB; Q9C0U6; -.
DR PaxDb; Q9C0U6; -.
DR PRIDE; Q9C0U6; -.
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; QHGTVFW; -.
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:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
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 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 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
