ID   XYLB_STRRU              Reviewed;         481 AA.
AC   P27156;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 66.
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   Streptomyces rubiginosus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces pseudogriseolus group.
OX   NCBI_TaxID=1929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1657868; DOI=10.1128/jb.173.21.6849-6858.1991;
RA   Wong H.C., Ting Y., Lin H.C., Reichert F., Myambo K., Watt K.W., Toy P.L.,
RA   Drummond R.J.;
RT   "Genetic organization and regulation of the xylose degradation genes in
RT   Streptomyces rubiginosus.";
RL   J. Bacteriol. 173:6849-6858(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; M73789; AAA26837.1; -; Genomic_DNA.
DR   PIR; A41339; A41339.
DR   AlphaFoldDB; P27156; -.
DR   SMR; P27156; -.
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   HAMAP; MF_02220; XylB; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR006000; Xylulokinase.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01312; XylB; 1.
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..481
FT                   /note="Xylulose kinase"
FT                   /id="PRO_0000059559"
FT   ACT_SITE        239
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT   BINDING         81..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT   SITE            13
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   481 AA;  49822 MW;  C39586CCC7124207 CRC64;
     MSAAEGPLVV GVDTSTQSTK ALVVDVATGR VVASGQAPHT VTSGAGRESD PRQWWDALCE
     ALRQCGEAAH EAAAVSIGGQ QHGLVTLDGH GEPVRPALLW NDVRSAPQGH RLIEELGGAK
     FWAERTGSVP AASFTVTKWA WLAEHEPEAV RATRAVRLPH DYLTERLTGQ GTTDRGDASG
     TGWWASGTEA YDEEILGHVG LDPALLPRVV RPGEVAGTVR DSHELPFSKG TLVACGTGDN
     AAAALGLGVR PGTPVMSLGT SGTVYAVTQR RPADPTGTVA GFADARGDWL PLACTLNCTL
     AVDRVAALLG LDREAVEPGH GVTLLPFLDG ERTPNLPRSS GLLHGLRHDT TGGQLLQAAY
     DGAVYSLLAA LDLVLDEDAD PSAPLLLIGG GARGTAWQQT VRRLSGRAVQ VPRAAELVAL
     GAAAQAAGLL TGEDPAAVAR RWETAAGPVL EAVERDEETL DRLAGVLSDA APLLERGTGA
     G