ID A0A078RU34_BACUN Unreviewed; 298 AA. AC A0A078RU34; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 22-FEB-2023, entry version 33. DE RecName: Full=Ribokinase {ECO:0000256|ARBA:ARBA00016943, ECO:0000256|HAMAP-Rule:MF_01987}; DE Short=RK {ECO:0000256|HAMAP-Rule:MF_01987}; DE EC=2.7.1.15 {ECO:0000256|ARBA:ARBA00012035, 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; Bacteroidota; 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 reaction CC requiring ATP and magnesium. The resulting D-ribose-5-phosphate can CC then be used either for sythesis of nucleotides, histidine, and CC tryptophan, or as a component of the pentose phosphate pathway. CC {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|ARBA:ARBA00000691, CC ECO:0000256|HAMAP-Rule:MF_01987}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01987}; CC Note=Requires a divalent cation, most likely magnesium in vivo, as an CC electrophilic catalyst to aid phosphoryl group transfer. It is the CC chelate of the metal and the nucleotide that is the actual substrate. CC {ECO:0000256|HAMAP-Rule:MF_01987}; CC -!- ACTIVITY REGULATION: Activated by a monovalent cation that binds near, CC but not in, the active site. The most likely occupant of the site in CC vivo is potassium. Ion binding induces a conformational change that may CC alter substrate affinity. {ECO:0000256|HAMAP-Rule:MF_01987}. CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5- CC phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000256|HAMAP- CC 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. Ribokinase CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01987}. CC -!- SIMILARITY: Belongs to the carbohydrate kinase pfkB family. CC {ECO:0000256|ARBA:ARBA00005380}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01987}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A078RU34; -. DR EnsemblBacteria; KDS47989; KDS47989; M094_2921. DR PATRIC; fig|1339349.3.peg.3975; -. 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-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 PANTHER; PTHR10584:SF166; RIBOKINASE; 1. DR PANTHER; PTHR10584; SUGAR KINASE; 1. DR Pfam; PF00294; PfkB; 1. DR PRINTS; PR00990; RIBOKINASE. DR SUPFAM; SSF53613; Ribokinase-like; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01987}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01987}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01987}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01987}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01987}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01987}. FT DOMAIN 1..293 FT /note="Carbohydrate kinase PfkB" FT /evidence="ECO:0000259|Pfam:PF00294" FT ACT_SITE 252 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 11..13 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 39..43 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 140 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 184 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 220..225 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 246 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 248 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 251..252 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 252 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 282 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 285 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 287 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 291 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule: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 //