ID   XYLB_ACTS3              Reviewed;         162 AA.
AC   P54271;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 53.
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   Actinoplanes sp. (strain ATCC 31351 / 3876) (Ampullariella sp.).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes; unclassified Actinoplanes.
OX   NCBI_TaxID=1872;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3027039; DOI=10.1128/jb.169.2.612-618.1987;
RA   Saari G.C., Kumar A.A., Kawasaki G.H., Insley M.Y., O'Hara P.J.;
RT   "Sequence of the Ampullariella sp. strain 3876 gene coding for xylose
RT   isomerase.";
RL   J. Bacteriol. 169:612-618(1987).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M15050; AAA92579.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54271; -.
DR   SMR; P54271; -.
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..>162
FT                   /note="Xylulose kinase"
FT                   /id="PRO_0000059546"
FT   REGION          16..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         162
SQ   SEQUENCE   162 AA;  16671 MW;  12CA622EAB7B2631 CRC64;
     MALVAGIGQL DAVVQGGHSA TPRPATGPAG PAAHSGRHQY DPDAWWARAT GDSREAGGLG
     RTLAAASVAG QQQRHGALLE SAVTVVRPAL LWNDTRRPGA AADLIQELGG ADKWAEAVGI
     VPVASLTLTN SGWLARHEPA NAAKVAAICL PHDWLTWKLS GS