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Database: UniProt/TrEMBL
Entry: B7N2J1_ECO81
LinkDB: B7N2J1_ECO81
Original site: B7N2J1_ECO81 
ID   B7N2J1_ECO81            Unreviewed;       309 AA.
AC   B7N2J1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   06-JUL-2016, entry version 51.
DE   RecName: Full=Ribokinase {ECO:0000256|HAMAP-Rule:MF_01987};
DE            Short=RK {ECO:0000256|HAMAP-Rule:MF_01987};
DE            EC=2.7.1.15 {ECO:0000256|HAMAP-Rule:MF_01987};
GN   Name=rbsK {ECO:0000256|HAMAP-Rule:MF_01987,
GN   ECO:0000313|EMBL:CAR10562.2};
GN   OrderedLocusNames=ECED1_4442 {ECO:0000313|EMBL:CAR10562.2};
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397 {ECO:0000313|EMBL:CAR10562.2, ECO:0000313|Proteomes:UP000000748};
RN   [1] {ECO:0000313|Proteomes:UP000000748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a {ECO:0000313|Proteomes:UP000000748};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA   Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA   Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA   Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA   Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA   Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA   Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a
CC       reaction requiring ATP and magnesium. The resulting D-ribose-5-
CC       phosphate can then be used either for sythesis of nucleotides,
CC       histidine, and tryptophan, or as a component of the pentose
CC       phosphate pathway. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-ribose = ADP + D-ribose 5-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01987};
CC       Note=Requires a divalent cation, most likely magnesium in vivo, as
CC       an electrophilic catalyst to aid phosphoryl group transfer. It is
CC       the chelate of the metal and the nucleotide that is the actual
CC       substrate. {ECO:0000256|HAMAP-Rule:MF_01987};
CC   -!- ENZYME REGULATION: Activated by a monovalent cation that binds
CC       near, but not in, the active site. The most likely occupant of the
CC       site in vivo is potassium. Ion binding induces a conformational
CC       change that may alter substrate affinity. {ECO:0000256|HAMAP-
CC       Rule:MF_01987}.
CC   -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose
CC       5-phosphate from beta-D-ribopyranose: step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       Ribokinase subfamily. {ECO:0000256|HAMAP-Rule:MF_01987}.
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DR   EMBL; CU928162; CAR10562.2; -; Genomic_DNA.
DR   RefSeq; WP_012601807.1; NC_011745.1.
DR   ProteinModelPortal; B7N2J1; -.
DR   EnsemblBacteria; CAR10562; CAR10562; ECED1_4442.
DR   KEGG; ecq:ECED1_4442; -.
DR   PATRIC; 38492950; VBIEscCol8292_4436.
DR   HOGENOM; HOG000235950; -.
DR   KO; K00852; -.
DR   OMA; NADHVIS; -.
DR   OrthoDB; EOG64JFMD; -.
DR   BioCyc; ECOL585397:GJCU-4484-MONOMER; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000000748; Chromosome.
DR   GO; GO:0004747; F:ribokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006014; P:D-ribose metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   HAMAP; MF_01987; Ribokinase; 1.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR011877; D_ribokin.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR002139; Ribo/fructo_kinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   Pfam; PF00294; PfkB; 1.
DR   PRINTS; PR00990; RIBOKINASE.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR02152; D_ribokin_bact; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000748};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|RuleBase:RU003704, ECO:0000256|SAAS:SAAS00446051,
KW   ECO:0000313|EMBL:CAR10562.2};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|RuleBase:RU003704, ECO:0000256|SAAS:SAAS00446022,
KW   ECO:0000313|EMBL:CAR10562.2}.
FT   DOMAIN        6    297       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     223    228       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   NP_BIND     254    255       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   REGION       14     16       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   REGION       42     46       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   ACT_SITE    255    255       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       249    249       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       251    251       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       285    285       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       288    288       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       290    290       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       294    294       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     143    143       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     187    187       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   BINDING     255    255       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     279    279       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
SQ   SEQUENCE   309 AA;  32292 MW;  55EF8F6B243014EF CRC64;
     MQNAGSLVVL GSINADHILN LQSFPTPGET VTGNHYQVAF GGKGANQAVA AGRSGANIAF
     IACTGDDSIG ESVRQQLATD NIDISPVSVI KGESTGVALI FVNGEGENVI GIHAGANAAL
     SPALVEAQRE RIANASALLM QLESPLESVM AAAKIAHQNK TIVALNPAPA RELPDELLAL
     VDIITPNETE AEKLTGIRVE NDEDAAKAAQ VLHEKGIRTV LITLGSRGVW ASVNGEGQRV
     PGFRVQAVDT IAAGDTFNGA LITSLLEEKP LPEAIRFAHA AAAIAVTRKG AQPSVPWREE
     IDAFLDRQR
//
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