ID A0A154P6D5_9HYME Unreviewed; 309 AA. AC A0A154P6D5; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 07-SEP-2016, entry version 3. DE RecName: Full=Ribokinase {ECO:0000256|HAMAP-Rule:MF_03215}; DE Short=RK {ECO:0000256|HAMAP-Rule:MF_03215}; DE EC=2.7.1.15 {ECO:0000256|HAMAP-Rule:MF_03215}; GN ORFNames=WN55_09393 {ECO:0000313|EMBL:KZC07401.1}; OS Dufourea novaeangliae. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Apoidea; Halictidae; Rophitinae; Dufourea. OX NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC07401.1, ECO:0000313|Proteomes:UP000076502}; RN [1] {ECO:0000313|EMBL:KZC07401.1, ECO:0000313|Proteomes:UP000076502} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0120121106 {ECO:0000313|EMBL:KZC07401.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:KZC07401.1}; RA Pan H., Kapheim K.; RT "The genome of Dufourea novaeangliae."; RL Submitted (JUL-2015) 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_03215}. CC -!- CATALYTIC ACTIVITY: ATP + D-ribose = ADP + D-ribose 5-phosphate. CC {ECO:0000256|HAMAP-Rule:MF_03215}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03215}; 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_03215}; 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_03215}. 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_03215}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03215}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215}. CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03215}. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. CC Ribokinase subfamily. {ECO:0000256|HAMAP-Rule:MF_03215}. 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; KQ434826; KZC07401.1; -; Genomic_DNA. DR RefSeq; XP_015428929.1; XM_015573443.1. DR GeneID; 107185697; -. DR UniPathway; UPA00916; UER00889. DR Proteomes; UP000076502; Unassembled WGS sequence. DR GO; GO:0004747; F:ribokinase activity; IEA:InterPro. DR GO; GO:0006014; P:D-ribose metabolic process; IEA:InterPro. 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; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03215}; KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_03215}; KW Complete proteome {ECO:0000313|Proteomes:UP000076502}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03215, KW ECO:0000256|RuleBase:RU003704, ECO:0000313|EMBL:KZC07401.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03215}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03215}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03215}; KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03215}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_03215}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03215, KW ECO:0000256|RuleBase:RU003704}. FT DOMAIN 3 299 PfkB. {ECO:0000259|Pfam:PF00294}. FT NP_BIND 221 226 ATP. {ECO:0000256|HAMAP-Rule:MF_03215}. FT NP_BIND 254 255 ATP. {ECO:0000256|HAMAP-Rule:MF_03215}. FT REGION 12 14 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03215}. FT REGION 40 44 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03215}. FT ACT_SITE 255 255 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_03215}. FT METAL 249 249 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_03215}. FT METAL 251 251 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_03215}. FT METAL 287 287 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_03215}. FT METAL 290 290 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_03215}. FT METAL 292 292 Potassium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_03215}. FT METAL 296 296 Potassium. {ECO:0000256|HAMAP-Rule: FT MF_03215}. FT BINDING 141 141 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03215}. FT BINDING 185 185 ATP. {ECO:0000256|HAMAP-Rule:MF_03215}. FT BINDING 242 242 ATP. {ECO:0000256|HAMAP-Rule:MF_03215}. FT BINDING 255 255 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03215}. SQ SEQUENCE 309 AA; 33002 MW; 7E346693EF1605E2 CRC64; MSPKIVVVGS CMIDFTSYSP RLPKSGETLV GSNFEIKYGG KGANQCVAAA KLGASTAIVA SLGSDVYAQE YLKIFKKENV NVAHVQIQEN QHSGIAHITV ADNGENHIVI VSGSNESLSL KHVDAAAEVV RDAAVLLCQF ETPLETTRHA LKLHKDHGLS IVNGAPAMEH VDYDLLSLCD IFCVNETEAE IMTGVQPLGL SNMQEAIDKL LDNGCNTVIL TLGKMGAAYA SRKNRTATLV PTRRVKPVDT TGAGDAFLGA IAYFKAYHPG LSMDECIRRA CVVATESVLK LGTHASFPTR SSLSPDLFV //