ID   XYLB_LACPE              Reviewed;         501 AA.
AC   P21939;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   24-JAN-2024, entry version 75.
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   Lactiplantibacillus pentosus (Lactobacillus pentosus).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MD353;
RX   PubMed=1660563; DOI=10.1007/bf00290664;
RA   Lokman B.C., van Santen P., Verdoes J.C., Kruese J., Leer R.J., Posno M.,
RA   Pouwels P.H.;
RT   "Organization and characterization of three genes involved in D-xylose
RT   catabolism in Lactobacillus pentosus.";
RL   Mol. Gen. Genet. 230:161-169(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=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: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; M57384; AAA25259.1; -; Genomic_DNA.
DR   PIR; S18562; S18562.
DR   AlphaFoldDB; P21939; -.
DR   SMR; P21939; -.
DR   STRING; 1589.GCA_001188985_00559; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0005998; P:xylulose catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07808; FGGY_D-XK_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; 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..501
FT                   /note="Xylulose kinase"
FT                   /id="PRO_0000059554"
FT   ACT_SITE        240
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT   BINDING         82..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT   SITE            9
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   501 AA;  54793 MW;  F6AB1C5941385B57 CRC64;
     MSAVVLGIDL GTSAVKVSAI DKQGNVVAQA SAKYALQQPH PGYSEQDPED WVTQTTQAIR
     ELLQQSEVTA DQIEGLSYSG QMHGLVLLDE SATVLRPAIL WNDTRTTSQC RELESQFGDD
     FIKITGNRPL EGFTLPKLLW VKENEPNIWK RARTFLLPKD YLRYRMTGKL AMDKSDATGT
     VLLDITTSQW SETLCNQLDI PLTLCPPLIE STAYVGHINQ TYAQLSGLSV NTKVFGGAAD
     NAAGAVGAGI LSSDKALVSI GTSGVVLKYE DNAQTDYRGV LQYERHAFPG KYYSMGVTLA
     AGYSLNWFKQ TFAPDEDFGT VVASAEQSTI GANGLLFAPY IVGERAPYAD ATIRGSFIGV
     DGSHQRADFV RAVLEGIIFS FEDLIKLYQH NGAEFKTIVS IGGGAKSALW LQIQADIFNC
     KVVSLKNEQG PGMGAAMIAA TGLGWFKTLA DCAQTFVHYG KAYYPVTAHV AQYQEMYRLY
     QQIYVQTQPI TAGLLEQRKQ H
//