ID A0A136Q090_9FIRM Unreviewed; 317 AA. AC A0A136Q090; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 02-NOV-2016, entry version 5. 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 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: 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: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 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-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; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987}; KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987}; KW Complete proteome {ECO:0000313|Proteomes:UP000070366}; 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: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:SAAS00446022}. FT DOMAIN 4 296 PfkB. {ECO:0000259|Pfam:PF00294}. FT NP_BIND 222 227 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}. FT NP_BIND 254 255 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}. FT REGION 41 45 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01987}. FT ACT_SITE 255 255 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01987}. FT METAL 251 251 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 288 288 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01987}. FT METAL 290 290 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01987}. FT BINDING 142 142 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01987}. FT BINDING 186 186 ATP. {ECO:0000256|HAMAP-Rule:MF_01987}. FT BINDING 255 255 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //