XYLB_STAES
ID XYLB_STAES Reviewed; 496 AA.
AC Q8CR47;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
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}; OrderedLocusNames=SE_2085;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05727.1; -; Genomic_DNA.
DR RefSeq; NP_765640.1; NC_004461.1.
DR RefSeq; WP_002485370.1; NZ_WBME01000013.1.
DR AlphaFoldDB; Q8CR47; -.
DR SMR; Q8CR47; -.
DR STRING; 176280.SE_2085; -.
DR EnsemblBacteria; AAO05727; AAO05727; SE_2085.
DR GeneID; 50017832; -.
DR KEGG; sep:SE_2085; -.
DR PATRIC; fig|176280.10.peg.2037; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_009281_3_0_9; -.
DR OMA; WHVMGVT; -.
DR Proteomes; UP000001411; Chromosome.
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..496
FT /note="Xylulose kinase"
FT /id="PRO_0000059555"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT BINDING 83..84
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT SITE 10
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
SQ SEQUENCE 496 AA; 55295 MW; 8C83A972C55D8FD1 CRC64;
MVKEVVLGID LGTSAIKIIA VDQLGNVIES VSETLKLYQE HPGYSEQDPN EWFEATKKGI
KELIQSTEMS DKIVKGISFS GQMHGLVIVD DNGIPLRKAI LWNDTRNSIQ CRQIEDIYGE
RLNYNPILEG FTLPKMLWVQ QHEPEIWNRV DVFMLPKDYL RYCLTQTIHM EYSDACSTLL
FNPENYEWTK DVGDTFNIGD IYPPLVKSHS YVGNVTSSLA KELGLSSDVA VYAGGGDNAC
GAIGAGVIHD KSALCSIGTS GVVLNVEYQR VTSYDSNLHL FNHSVPDTYY AMGVTLAAGY
SLNWLKQTFF ENESFEEILN LAASSKIGAN GLLFTPYLAG ERTPHGDAQI RGSFIGISGQ
HTKADFARAV IEGITYSLYD SIKIMRRAGH EMNSITSIGG GAKSRFWLQL QADIFNVQIK
RLKHEEGPSM GAAILAAYGL GWFKTIESCV EAFIKVDEVF EPNNENHDLY EQYYSVYEAI
YKQTKQLTAD LLTITN