ID A0A136Q090_9FIRM Unreviewed; 317 AA. AC A0A136Q090; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 17-JUN-2020, entry version 20. 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 ORFNames=HMPREF3293_03159 {ECO:0000313|EMBL:KXK64111.1}; OS Christensenella minuta. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Christensenellaceae; OC Christensenella. OX NCBI_TaxID=626937 {ECO:0000313|EMBL:KXK64111.1, ECO:0000313|Proteomes:UP000070366}; RN [1] {ECO:0000313|EMBL:KXK64111.1, ECO:0000313|Proteomes:UP000070366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22607 {ECO:0000313|EMBL:KXK64111.1, RC ECO:0000313|Proteomes:UP000070366}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) 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|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 -!- 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:KXK64111.1}. 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; LSZW01000067; KXK64111.1; -; Genomic_DNA. DR RefSeq; WP_066740114.1; NZ_MAIR01000010.1. DR EnsemblBacteria; KXK64111; KXK64111; HMPREF3293_03159. DR KEGG; cmiu:B1H56_13500; -. DR PATRIC; fig|626937.4.peg.3110; -. DR KO; K00852; -. DR BioCyc; GCF_001571425-HMP:HMPREF3293_RS13805-MONOMER; -. DR BioCyc; GCF_001652705:A5N82_RS13350-MONOMER; -. DR UniPathway; UPA00916; UER00889. DR Proteomes; UP000070366; 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 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; 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|HAMAP-Rule:MF_01987, ECO:0000256|RuleBase:RU003704, KW ECO:0000256|SAAS:SAAS00471813, ECO:0000313|EMBL:KXK64111.1}; 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:UP000070366}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01987, KW ECO:0000256|RuleBase:RU003704, ECO:0000256|SAAS:SAAS00471907}. FT DOMAIN 4..296 FT /note="PfkB" FT /evidence="ECO:0000259|Pfam:PF00294" FT NP_BIND 222..227 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT NP_BIND 254..255 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT REGION 41..45 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT ACT_SITE 255 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT METAL 251 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT METAL 285 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT METAL 288 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT METAL 290 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 142 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 186 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" FT BINDING 255 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987" SQ SEQUENCE 317 AA; 33899 MW; CC4FC392622E7FFB CRC64; MNEKKITVIG HYGMSLLMDV ERFPAVGETV EGLGLVTEPG GKGYNQAIAA SRLGAEVNFI TAVGDDEFGA LCGKDLVSEG VQGRYIIPFE GQRTACAFVI NSADKCSEVY VYPGAIRKVT GAHIRRYADV IAQSGLLLLQ NEITVEALME AVDIAREAGV EVIYNPAPAR ELPAEAFPHI TCITPNETEA AILTGADPDA PLNVERAISL LHGKGAKNVI ITLGGNGSAV SLENGRTHRV NSLKVDVVST TGAGDSYNAA FAVRYMETRD ILESAKYAAV ASGLQVMRPG VIANMPYRQE ADAWFAEHKD EMEREEG //