(data stored in SCRATCH zone)

SWISSPROT: B1VNF6_STRGG

ID   B1VNF6_STRGG            Unreviewed;       305 AA.
AC   B1VNF6;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   07-JUN-2017, entry version 60.
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   OrderedLocusNames=SGR_150 {ECO:0000313|EMBL:BAG16979.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG16979.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG16979.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01987}.
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DR   EMBL; AP009493; BAG16979.1; -; Genomic_DNA.
DR   RefSeq; WP_012377562.1; NC_010572.1.
DR   ProteinModelPortal; B1VNF6; -.
DR   STRING; 455632.SGR_150; -.
DR   EnsemblBacteria; BAG16979; BAG16979; SGR_150.
DR   GeneID; 6214772; -.
DR   KEGG; sgr:SGR_150; -.
DR   PATRIC; fig|455632.4.peg.134; -.
DR   eggNOG; ENOG4108RVA; Bacteria.
DR   eggNOG; COG0524; LUCA.
DR   HOGENOM; HOG000235950; -.
DR   KO; K00852; -.
DR   OMA; AGMARFP; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004747; F:ribokinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd01174; ribokinase; 1.
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   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1VNF6.
DR   SWISS-2DPAGE; B1VNF6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|RuleBase:RU003704, ECO:0000256|SAAS:SAAS00644883,
KW   ECO:0000313|EMBL:BAG16979.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000001685};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|RuleBase:RU003704, ECO:0000256|SAAS:SAAS00644976}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    305       Ribokinase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002769913.
FT   DOMAIN        3    293       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     218    223       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   NP_BIND     250    251       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   REGION       38     42       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   ACT_SITE    251    251       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       245    245       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       247    247       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       281    281       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       284    284       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       286    286       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   BINDING     138    138       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     182    182       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   BINDING     251    251       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
SQ   SEQUENCE   305 AA;  30771 MW;  E5D45EAFAE167794 CRC64;
     MKIAVVGSYG AGLTMRVPKA PAAGETVSGG LFDSGAGGKG SNQAVGAARL GAEVALLTAV
     GDDEFGRAAR ELWRREGVSV EHVITAGAPT MVGFILVEPS GENRIAIAPG ALDELDAAAV
     DAFRAEIACA DVLVVSMEIP EEAVVAALRA GRESGTRTLL NPAPARPLPD ACWPLVDVLT
     PNQTEAPVLL GLDEGHGLGD EDLARALRER TGGTVVITRG GEGALVAQDT GVTAVPPHPA
     RTVVDTTGAG DSFTAAFAVA LAEGRPVDRA VEYATVAGAH TVSIAGVIPA LPTRAQLNAR
     IGSAS
//

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