ID A0A078RU34_BACUN Unreviewed; 298 AA. AC A0A078RU34; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 18-JAN-2017, entry version 16. 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:KDS47989.1}; GN ORFNames=M094_2921 {ECO:0000313|EMBL:KDS47989.1}; OS Bacteroides uniformis str. 3978 T3 ii. OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=1339349 {ECO:0000313|EMBL:KDS47989.1, ECO:0000313|Proteomes:UP000028013}; RN [1] {ECO:0000313|EMBL:KDS47989.1, ECO:0000313|Proteomes:UP000028013} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3978 T3 ii {ECO:0000313|EMBL:KDS47989.1, RC ECO:0000313|Proteomes:UP000028013}; RA Sears C., Carroll K., Sack B.R., Qadri F., Myers L.L., Chung G.-T., RA Escheverria P., Fraser C.M., Sadzewicz L., Shefchek K.A., Tallon L., RA Das S.P., Daugherty S., Mongodin E.F.; RL Submitted (APR-2014) 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: 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}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KDS47989.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JNHN01000184; KDS47989.1; -; Genomic_DNA. DR RefSeq; WP_035447294.1; NZ_JNHN01000184.1. DR EnsemblBacteria; KDS47989; KDS47989; M094_2921. DR UniPathway; UPA00916; UER00889. DR Proteomes; UP000028013; Unassembled WGS sequence. 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 TIGRFAMs; TIGR02152; D_ribokin_bact; 1. DR PROSITE; PS00583; PFKB_KINASES_1; 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:UP000028013}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01987, KW ECO:0000256|SAAS:SAAS00644883, ECO:0000313|EMBL:KDS47989.1}; 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|SAAS:SAAS00644976, ECO:0000313|EMBL:KDS47989.1}. FT DOMAIN 1 293 PfkB. {ECO:0000259|Pfam:PF00294}. FT NP_BIND 220 225 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}. FT NP_BIND 251 252 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}. FT REGION 11 13 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01987}. FT REGION 39 43 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01987}. FT ACT_SITE 252 252 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01987}. FT METAL 246 246 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01987}. FT METAL 248 248 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01987}. FT METAL 282 282 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 287 287 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01987}. FT METAL 291 291 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_01987}. FT BINDING 140 140 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01987}. FT BINDING 184 184 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}. FT BINDING 252 252 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01987}. SQ SEQUENCE 298 AA; 31927 MW; A46DDDB99B87EC35 CRC64; MKKIIVIGSS NVDMVVRTSH LPAPGETILG GEFFMNQGGK GANQAVAIKR LGGNLIFMAK LGNDVLGRQS VGYFKKEGID TRYIALDEDS ASGVALISVD DHAENSIVVA SGANMLLNEQ DVDKMLEEMC EGDILLMQLE IPLQTVEYAA RKAFGKGVKV VLNPAPARSL PKELFRHLYM VTPNRIEAEM LTGIKIANDA DVEKVAEEIC AMGVKNVIIT LGSKGCLIRE EGVSYRIDAF KVEPVDTTAA GDTFNGALCV GLSEGMDLKQ AAVMASKASS IAVTRMGAQS SIPYREEL //