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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}.
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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
 
 
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