(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BI12_GEOS0

ID   A0A0F6BI12_GEOS0        Unreviewed;       298 AA.
AC   A0A0F6BI12;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 25.
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=GY4MC1_0214 {ECO:0000313|EMBL:ADP73063.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73063.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73063.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73063.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:
CC       Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+);
CC         Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216;
CC         EC=2.7.1.15; Evidence={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   -!- ACTIVITY 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; CP002293; ADP73063.1; -; Genomic_DNA.
DR   RefSeq; WP_013399869.1; NC_014650.1.
DR   EnsemblBacteria; ADP73063; ADP73063; GY4MC1_0214.
DR   KEGG; gmc:GY4MC1_0214; -.
DR   KO; K00852; -.
DR   OMA; DIVLIQQ; -.
DR   OrthoDB; 1030724at2; -.
DR   BioCyc; GSP581103:G1GOQ-256-MONOMER; -.
DR   UniPathway; UPA00916; UER00889.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004747; F:ribokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-UniRule.
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   TIGRFAMs; TIGR02152; D_ribokin_bact; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BI12.
DR   SWISS-2DPAGE; A0A0F6BI12.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
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:ADP73063.1};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_01987,
KW   ECO:0000256|RuleBase:RU003704, ECO:0000256|SAAS:SAAS00061368}.
FT   DOMAIN        6    282       PfkB. {ECO:0000259|Pfam:PF00294}.
FT   NP_BIND     208    213       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   NP_BIND     239    240       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   REGION       13     15       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   REGION       41     45       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01987}.
FT   ACT_SITE    240    240       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       234    234       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   METAL       236    236       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       270    270       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       273    273       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   METAL       275    275       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   BINDING     141    141       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     185    185       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
FT   BINDING     240    240       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01987}.
FT   BINDING     264    264       ATP. {ECO:0000256|HAMAP-Rule:MF_01987}.
SQ   SEQUENCE   298 AA;  31847 MW;  FD97FD1F0AEC81CC CRC64;
     MTKPVITVVG SINMDLVTIA SRFPSQGETI LGEEFHLIPG GKGANQAVAA ARLGAEVHMI
     GAVGTDPFGN ELLRSLEREG VHIDNVKPVT HKGTGIASIT ILEQDNRIIV VPGANHALRP
     EDIDRYEEII AKSDVCVLQL EIPLSVVERA VFLAKKHHVR VILNPAPAQP LPQKLIEQAD
     FLTPNEHERE IIFEQVDVDV FADKVIVTEG ARGVTIRKDG KQVLIPSFCV PVVDTTGAGD
     TFNGALAVAL SKGMSLEDAC RFANAAAALS VTKLGAQGGM PTEEEVKKFL QEKAGCSS
//

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