(data stored in SCRATCH zone)

SWISSPROT: C1ARR9_RHOOB

ID   C1ARR9_RHOOB            Unreviewed;       510 AA.
AC   C1ARR9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   30-AUG-2017, entry version 51.
DE   RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU364073};
DE            Short=Xylulokinase {ECO:0000256|RuleBase:RU364073};
DE            EC=2.7.1.17 {ECO:0000256|RuleBase:RU364073};
GN   Name=xylB {ECO:0000256|RuleBase:RU364073,
GN   ECO:0000313|EMBL:BAH48746.1};
GN   OrderedLocusNames=ROP_04990 {ECO:0000313|EMBL:BAH48746.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48746.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48746.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48746.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + D-xylulose = ADP + D-xylulose 5-
CC       phosphate. {ECO:0000256|RuleBase:RU364073}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|RuleBase:RU003733}.
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DR   EMBL; AP011115; BAH48746.1; -; Genomic_DNA.
DR   RefSeq; WP_012687753.1; NC_012522.1.
DR   ProteinModelPortal; C1ARR9; -.
DR   STRING; 632772.ROP_04990; -.
DR   EnsemblBacteria; BAH48746; BAH48746; ROP_04990.
DR   KEGG; rop:ROP_04990; -.
DR   PATRIC; fig|632772.20.peg.552; -.
DR   eggNOG; ENOG4105CMG; Bacteria.
DR   eggNOG; COG1070; LUCA.
DR   HOGENOM; HOG000222138; -.
DR   KO; K00854; -.
DR   OMA; FSDAMHF; -.
DR   OrthoDB; POG091H073O; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005997; P:xylulose metabolic process; IEA:InterPro.
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   TIGRFAMs; TIGR01312; XylB; 1.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ARR9.
DR   SWISS-2DPAGE; C1ARR9.
KW   ATP-binding {ECO:0000256|RuleBase:RU364073};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU364073};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000256|SAAS:SAAS00430777,
KW   ECO:0000313|EMBL:BAH48746.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364073};
KW   Transferase {ECO:0000256|RuleBase:RU003733,
KW   ECO:0000256|SAAS:SAAS00193248, ECO:0000313|EMBL:BAH48746.1};
KW   Xylose metabolism {ECO:0000256|RuleBase:RU364073}.
FT   DOMAIN        8    248       FGGY_N. {ECO:0000259|Pfam:PF00370}.
FT   DOMAIN      263    452       FGGY_C. {ECO:0000259|Pfam:PF02782}.
SQ   SEQUENCE   510 AA;  54512 MW;  291A997218B5E579 CRC64;
     MTTAARVHLG VDIGTSSCKV VAVDHTGAVM TTAVREYPLF SDRHGWSEQD PHDWWAATDA
     CIREVTAQLP RRGDEIVAIG LSGQMHGLVA LDDTGTVIRR AILWNDQRCE AECVAITDTV
     GGPHSVLDAT ANRLITGFTA GKVAWLRDHE PEVFARIHRI VNPKDYLRLR MNGRFVTDVS
     EASGTGLFDV ANRKWSPAML DAVGVSESML PEVVESPERT GVLLPEIADA WNLRPDVEVY
     GGGGDAVVQT ASMGITQRGD IGVTLGTAGI VAAVSRTCPD NVTGSVQVSC YNQPGFWHVM
     GVSLSAAGGL QWLADVVHQL PGAQDVSFTE LIDLAKEVPV GADGLLFLPY LAGERSPHYA
     PSASGAMVGL TRMHGLGHLV RAVIEGALLN MRQILESFAD LGIPCDRIIA SGGATRDAFW
     LQAMADVFGT EVVTMTGSSE GGAYGAAIVS GVGAGTWESF DDAYGHLQVS SRHVPRTAEA
     ARYTRIFEGY RNLFGHFTDV FGDIDIARKT
//

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