ID A0A154P6D5_DUFNO Unreviewed; 309 AA. AC A0A154P6D5; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 29-MAY-2024, entry version 31. DE RecName: Full=Ribokinase {ECO:0000256|ARBA:ARBA00016943, ECO:0000256|HAMAP-Rule:MF_03215}; DE Short=RK {ECO:0000256|HAMAP-Rule:MF_03215}; DE EC=2.7.1.15 {ECO:0000256|ARBA:ARBA00012035, ECO:0000256|HAMAP-Rule:MF_03215}; GN ORFNames=WN55_09393 {ECO:0000313|EMBL:KZC07401.1}; OS Dufourea novaeangliae (Sweat bee). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; OC Anthophila; 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 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_03215}. 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_03215}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03215}; 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_03215}; 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_03215}. 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_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. Ribokinase CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03215}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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 AlphaFoldDB; A0A154P6D5; -. DR STRING; 178035.A0A154P6D5; -. DR EnsemblMetazoa; XM_015573443.1; XP_015428929.1; LOC107185697. DR GeneID; 107185697; -. DR OrthoDB; 1217765at2759; -. DR UniPathway; UPA00916; UER00889. DR Proteomes; UP000076502; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; 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 NCBIfam; TIGR02152; D_ribokin_bact; 1. 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 PROSITE; PS00584; PFKB_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03215}; Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_03215}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03215}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03215}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03215}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03215}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03215}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_03215}; KW Reference proteome {ECO:0000313|Proteomes:UP000076502}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03215}. FT DOMAIN 4..299 FT /note="Carbohydrate kinase PfkB" FT /evidence="ECO:0000259|Pfam:PF00294" FT ACT_SITE 255 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 12..14 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 40..44 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 141 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 185 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 221..226 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 242 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 249 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 251 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 254..255 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 255 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 287 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 290 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 292 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03215" FT BINDING 296 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule: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 //