AC MF_01987; DC Protein; auto c? or TR HAMAP; MF_01987; -; 1; level=0 XX Names: Ribokinase XX case ID DEOK DE RecName: Full=Deoxyribokinase; DE Short=dRK; DE EC=2.7.1.229; DE AltName: Full=ATP:2-deoxy-D-ribose 5-phosphotransferase; GN Name=deoK; else ID RBSK DE RecName: Full=Ribokinase; DE Short=RK; DE EC=2.7.1.15; GN Name=rbsK; end case XX case CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of 2-deoxy-D- CC ribose to 2-deoxy-D-ribose 5-phosphate (dRib-5P), allowing the use of CC deoxyribose as the sole carbon source. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-deoxy-D-ribose + ATP = 2-deoxy-D-ribose 5-phosphate + ADP + CC H(+); Xref=Rhea:RHEA:30871, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:62877, ChEBI:CHEBI:90761, ChEBI:CHEBI:456216; CC EC=2.7.1.229; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. CC Deoxyribokinase subfamily. else 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 -!- 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; 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 -!- 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. CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5- CC phosphate from beta-D-ribopyranose: step 2/2. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase CC subfamily. end case CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. XX DR PROSITE; PS00584; PFKB_KINASES_2; 1; trigger=no DR Pfam; PF00294; PfkB; 1; trigger=no DR PRINTS; PR00990; RIBOKINASE; 1; trigger=no DR NCBIfam; TIGR02152; D_ribokin_bact; 1; trigger=no XX KW ATP-binding KW Carbohydrate metabolism KW Cytoplasm KW Kinase KW Magnesium KW Metal-binding KW Nucleotide-binding KW Transferase KW Potassium XX GO GO:0005737; C:cytoplasm GO GO:0005524; F:ATP binding case not GO GO:0004747; F:ribokinase activity end case GO GO:0046835; P:carbohydrate phosphorylation case not GO GO:0019303; P:D-ribose catabolic process end case XX FT From: DEOK_SALTI (P0DX97) FT SITE 10 FT /note="Important for substrate specificity" FT Tag: deoxyribokinase; Optional; Condition: M FT From: RBSK_ECOLI (P0A9J6) FT BINDING 223..228 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: x(2)-G-x(2)-G FT BINDING 254..255 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-D FT BINDING 14..16 FT /ligand="substrate" FT Condition: x(2)-D FT BINDING 42..46 FT /ligand="substrate" FT Condition: G-[KR]-[GAS]-x-[NR] FT ACT_SITE 255 FT /note="Proton acceptor" FT Condition: D FT BINDING 249 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT Optional; Condition: [DN] FT BINDING 251 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT BINDING 285 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT BINDING 288 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT BINDING 290 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT Optional; Condition: G FT BINDING 294 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT Optional; Condition: S FT BINDING 143 FT /ligand="substrate" FT Optional; Condition: E FT BINDING 187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: N FT BINDING 255 FT /ligand="substrate" FT Condition: D FT BINDING 279 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: [HN] XX Size: 259-382; Related: None; Template: P0A9J6; A0A0H2WZY4; P0DX97; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: Met-10 in Salmonella deoxyribokinase corresponds to Asn-14 in E.coli ribokinase. It is a key residue differentiating ribose and deoxyribose (PubMed=10648508). XX # Revision 1.11 2023/11/07 //