ID   XYLB_ARTS7              Reviewed;          96 AA.
AC   P26909;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 59.
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};
DE   Flags: Fragment;
GN   Name=xylB {ECO:0000255|HAMAP-Rule:MF_02220};
OS   Arthrobacter sp. (strain NRRL B3728).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1854339; DOI=10.1042/bj2770263;
RA   Loviny-Anderton T., Shaw P.C., Shin M.K., Hartley B.S.;
RT   "D-xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728.
RT   Gene cloning, sequence and expression.";
RL   Biochem. J. 277:263-271(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; X59466; CAA42074.1; -; Genomic_DNA.
DR   AlphaFoldDB; P26909; -.
DR   SMR; P26909; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   Pfam; PF00370; FGGY_N; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Transferase; Xylose metabolism.
FT   CHAIN           1..>96
FT                   /note="Xylulose kinase"
FT                   /id="PRO_0000059547"
FT   BINDING         71..72
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"
FT   NON_TER         96
SQ   SEQUENCE   96 AA;  10006 MW;  1B812D5E616DB7F1 CRC64;
     MTLVAGIDSS TQSCKVVIRD ADTGVLIRSS RASHPDGTEV DPEFWFDALQ EAIAQAGGLD
     DVAAISVGGQ QHGMVALDAT GAVIRPALLW NDNRSA