ID   XYLB_STAXY              Reviewed;         483 AA.
AC   P27155;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   02-SEP-2026, entry version 79.
DE   RecName: Full=Xylulose kinase {ECO:0000255|HAMAP-Rule:MF_02220};
DE            Short=Xylulokinase {ECO:0000255|HAMAP-Rule:MF_02220};
DE            EC=2.7.1.17 {ECO:0000255|HAMAP-Rule:MF_02220};
GN   Name=xylB {ECO:0000255|HAMAP-Rule:MF_02220};
OS   Staphylococcus xylosus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 20267 / Isolate C2A;
RX   PubMed=1714034; DOI=10.1007/bf00273926;
RA   Sizemore C., Buchner E., Rygus T., Witke C., Goetz F., Hillen W.;
RT   "Organization, promoter analysis and transcriptional regulation of the
RT   Staphylococcus xylosus xylose utilization operon.";
RL   Mol. Gen. Genet. 227:377-384(1991).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_02220}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-xylulose + ATP = D-xylulose 5-phosphate + ADP + 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:0000255|HAMAP-Rule:MF_02220};
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_02220, ECO:0000305}.
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DR   EMBL; X57599; CAA40825.1; -; Genomic_DNA.
DR   PIR; S16531; S16531.
DR   AlphaFoldDB; P27155; -.
DR   SMR; P27155; -.
DR   STRING; 1288.AWC37_11475; -.
DR   PaxDb; 1288-AWC37_11475; -.
DR   eggNOG; COG1070; Bacteria.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004856; F:D-xylulokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005998; P:xylulose catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07808; ASKHA_NBD_FGGY_EcXK-like; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_02220; XylB; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR050406; FGGY_Carb_Kinase.
DR   InterPro; IPR018484; FGGY_N.
DR   InterPro; IPR006000; Xylulokinase.
DR   NCBIfam; TIGR01312; XylB; 1.
DR   PANTHER; PTHR43095; SUGAR KINASE; 1.
DR   PANTHER; PTHR43095:SF5; 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.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Transferase; Xylose metabolism.
FT   CHAIN           1..483
FT                   /note="Xylulose kinase"
FT                   /id="PRO_0000059557"
FT   BINDING         79..80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT   SITE            8
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   483 AA;  53953 MW;  7758D359B6DC8CC2 CRC64;
     MAYVIGIDIG TSALKTLVVN KSGDVVESYS VSYNTAHPKS GYSEIDPEIW YEATLESLKY
     ILNHYTHNDL TGISFSGQMH GLVVIDQEGN PIRPAILWND TRTSQEVEDI KKNLGLNSLL
     QLTQNTVLEG FTLPKLMWLK NHEQDNYKRI YKFMLPKDYI VYKLTGNVYT EPSDAAGTIM
     FSVKDENWST ELLHRLNIDP SICPEIIASH QKSGQLTEKV KNTLGIDSNI NVYQGGANNA
     CGALGSGITD EQKQLVSIGT SGVALSIENS TDYENDGNVH YFNHCVPNQK YIMGVTLSAG
     YSLEWLKQLI SADENFTTFL KDINQSEVGA NGLMYTPYLL GERTPHNDAS VRGSFIGLDA
     NTTQLDMKRA VIEGITYSIN ESIHIMKNNA ININEIVSIG GGAKNNQWLQ IQADIFNTTI
     TTRTEEQGPA YGAAMIAAMG EQWFNTFNEM SEAWIAYHQK VYPIETNTKS YQDLFNIYKT
     IYD
//