ID   XYLB_RAT                Reviewed;         536 AA.
AC   Q3MIF4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=Xylulose kinase;
DE            Short=Xylulokinase;
DE            EC=2.7.1.17;
GN   Name=Xylb;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Phosphorylates D-xylulose to produce D-xylulose 5-phosphate,
CC       a molecule that may play an important role in the regulation of glucose
CC       metabolism and lipogenesis. {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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR   EMBL; BC101852; AAI01853.1; -; mRNA.
DR   RefSeq; NP_001028876.1; NM_001033704.1.
DR   AlphaFoldDB; Q3MIF4; -.
DR   SMR; Q3MIF4; -.
DR   STRING; 10116.ENSRNOP00000019106; -.
DR   PhosphoSitePlus; Q3MIF4; -.
DR   PaxDb; 10116-ENSRNOP00000019106; -.
DR   PeptideAtlas; Q3MIF4; -.
DR   GeneID; 316067; -.
DR   KEGG; rno:316067; -.
DR   UCSC; RGD:1307372; rat.
DR   AGR; RGD:1307372; -.
DR   CTD; 9942; -.
DR   RGD; 1307372; Xylb.
DR   eggNOG; KOG2531; Eukaryota.
DR   InParanoid; Q3MIF4; -.
DR   OrthoDB; 1704034at2759; -.
DR   PhylomeDB; Q3MIF4; -.
DR   Reactome; R-RNO-5661270; Formation of xylulose-5-phosphate.
DR   PRO; PR:Q3MIF4; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004856; F:xylulokinase activity; ISS:UniProtKB.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR   GO; GO:0005997; P:xylulose metabolic process; ISS:UniProtKB.
DR   CDD; cd07776; FGGY_D-XK_euk; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
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   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase; Xylose metabolism.
FT   CHAIN           1..536
FT                   /note="Xylulose kinase"
FT                   /id="PRO_0000230988"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         441..442
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         445
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   536 AA;  57970 MW;  39206405B8361CB4 CRC64;
     MAERAGRRCC LGWDFSTQQV KVVAVDAELN VFYEDSVHFD RDLPEFGTQG GVHVHKDRLT
     VTSPVLMWVQ ALDLILEKMK ASGFDFSQVL ALSGAGQQHG SVYWKTGASL ALSSLSPALL
     LHQQLQACFS VSDCPIWMDS STTAQCHQLE AAVGGAQALS CLTGSRAYER FTGNQISKIF
     QKNPEAYSNS ERISLVSSFA ASLFLGRYSP IDYSDGSGMN LLQIQEKVWS QACLDACAPH
     LKEKLGSPVP SCSVVGAISS YYVQRYGFPP GCKVVAFTGD NPASLAGMRL EEGDVAVSLG
     TSDTLFLWLQ KPMPALEGHI FCNPVDARQY MALLCFKNGS LMREKIRDES ASCSWNKFSK
     ALQSTEMGNN GNLGFYFDVM EITPEIIGCH RFNADNMEVS AFPGDVEIRA LVEGQFMAKR
     IHAEGLGYRI MPKTKILATG GASHNKDILQ VLADVFGAPV YVIDTTSSAC VGSAYRAFHG
     LAGGTGVAFS EVVKSAPQPS LAATPNPGAS QVYAALLPRY AELEQRILSK ARGPLE
//