XYLB_STRCO
ID XYLB_STRCO Reviewed; 481 AA.
AC Q9RK00; Q9L0B7;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 102.
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=SCO1170;
GN ORFNames=2SCG11.04c, SCG11A.01;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939108; CAD55165.1; -; Genomic_DNA.
DR RefSeq; NP_733525.1; NC_003888.3.
DR RefSeq; WP_011027626.1; NZ_VNID01000006.1.
DR AlphaFoldDB; Q9RK00; -.
DR SMR; Q9RK00; -.
DR STRING; 100226.SCO1170; -.
DR GeneID; 1096593; -.
DR KEGG; sco:SCO1170; -.
DR PATRIC; fig|100226.15.peg.1168; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_009281_12_0_11; -.
DR InParanoid; Q9RK00; -.
DR OMA; HILLPHD; -.
DR PhylomeDB; Q9RK00; -.
DR Proteomes; UP000001973; 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 Reference proteome; Transferase; Xylose metabolism.
FT CHAIN 1..481
FT /note="Xylulose kinase"
FT /id="PRO_0000059558"
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; 49682 MW; 69682F3AD2EEBD03 CRC64;
MSAAEGPLVV GVDTSTQSTK ALVVDAATGR VVASGQAPHT VSSGTGRESD PRQWWDALGE
ALSQCGEAAR EAAAVSVGGQ QHGLVTLDAR GEPVRPALLW NDVRSAPQAR RLIDELGGAK
AWAERTGSVP SASFTVTKWA WLTEHEPEAA RAVKAVRLPH DYLTERLTGE GTTDRGDVSG
TGWWASGTEA YDEEILARVA LDPALLPRVV RPGEVAGTVR DGHGLPFSKG TLVAAGTGDN
AAAALGLGLR PGVPVMSLGT SGTAYAVSQR RPADPTGTVA GFADARGDWL PLACTLNCTL
AVDRVASLLG LDREAVEPGT DVTLLPFLDG ERTPNLPHSS GLLHGLRHDT TAGQLLQAAY
DGAVHSLLGA LDLVLDADAD PSAPLLLIGG GARGTAWQQT VRRLSGRPVQ IPEARELVAL
GAAAQAAGLL TGEDAAAVAR RWNTAAGPVL DAVERDEATL NRITGVLSDA APLLERDAAS
R