ID   XYLB_KLEPN              Reviewed;         483 AA.
AC   P29444;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   24-JAN-2024, entry version 76.
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   Klebsiella pneumoniae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1033-5P14 / KAY2026;
RX   PubMed=1324398; DOI=10.1007/bf00283840;
RA   Feldmann S.D., Sahm H., Sprenger G.A.;
RT   "Cloning and expression of the genes for xylose isomerase and xylulokinase
RT   from Klebsiella pneumoniae 1033 in Escherichia coli K12.";
RL   Mol. Gen. Genet. 234:201-210(1992).
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; X61059; CAA43390.1; -; Genomic_DNA.
DR   PIR; S25070; S25070.
DR   AlphaFoldDB; P29444; -.
DR   SMR; P29444; -.
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:SF6; 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_0000059551"
FT   ACT_SITE        233
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT   BINDING         77..78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT   SITE            6
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   483 AA;  51907 MW;  835FF494018FE872 CRC64;
     MYIGIDLGTS GVKAILLNEQ GEVVASHTEK LTVSRPHPLW SEQDPEQWWL ATDTAMKALG
     AHDSLRHVKG LGIAGQMHGA TLLDKSLQVL RPAILWNDGR CAEECQLLED KVSASRQITG
     NLMMPGFTAP KLLWVQRHEA AVFSQVDKVL LPKDYLRLRM TGELASDMSD AAGTMWLDVA
     RRDWSDEMLA ACDLSRDAMP ALFEGSDVTG QLRPEVAQAW NMPPALVVGG GGDNAAGAVG
     IGMADAGQAM LSLGTSGVYF AVSEGFLSKP ESAVHSFCHA CRGRWHLMSV MLSAASCLDW
     AAKLTGLASV PALIAAAQTA DESAGPVWFL PYLSGERTPH NNPQAKGVFF GLTHQHGPAE
     LARAVLEGVG YALADGMDVV HACAIKPEAI TLIGGGRARY WRQMLADISG LQLDYRTGGD
     VGPALGAARL AHVAVHDEAD RPGLLKPLPL EQAHRPDDRR VAHYAPQREI FARIFSKLKP
     LMS
//