AC MF_02128; DC Protein; auto TR HAMAP; MF_02128; -; 1; level=0 XX Names: TMP_kinase XX ID THIL DE RecName: Full=Thiamine-monophosphate kinase; DE Short=TMP kinase; DE Short=Thiamine-phosphate kinase; DE EC=2.7.4.16; GN Name=thiL; XX CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine- CC monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active CC form of vitamin B1. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + thiamine phosphate = ADP + thiamine diphosphate; CC Xref=Rhea:RHEA:15913, ChEBI:CHEBI:30616, ChEBI:CHEBI:37575, CC ChEBI:CHEBI:58937, ChEBI:CHEBI:456216; EC=2.7.4.16; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine diphosphate from thiamine phosphate: step 1/1. CC -!- MISCELLANEOUS: Reaction mechanism of ThiL seems to utilize a direct, CC inline transfer of the gamma-phosphate of ATP to TMP rather than a CC phosphorylated enzyme intermediate. CC -!- SIMILARITY: Belongs to the thiamine-monophosphate kinase family. XX DR Pfam; PF00586; AIRS; 1; trigger=no DR Pfam; PF02769; AIRS_C; 1; trigger=no DR NCBIfam; TIGR01379; ThiL; 1; trigger=no DR PIRSF; PIRSF005303; Thiam_monoph_kin; 1; trigger=no XX KW ATP-binding KW Kinase KW Magnesium KW Metal-binding KW Nucleotide-binding KW Thiamine biosynthesis KW Transferase XX GO GO:0000287; F:magnesium ion binding GO GO:0005524; F:ATP binding GO GO:0009030; F:thiamine-phosphate kinase activity GO GO:0009229; P:thiamine diphosphate biosynthetic process XX FT From: THIL_AQUAE (O67883) FT BINDING 118..119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-[ND] FT BINDING 27 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT Condition: [DE] FT BINDING 27 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT Condition: [DE] FT BINDING 41 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT Condition: [TS] FT BINDING 42 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: [TS] FT BINDING 43 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: D FT BINDING 43 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 71 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 71 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT Condition: D FT BINDING 71 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT Condition: D FT BINDING 119 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: [ND] FT BINDING 207 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT Condition: D FT BINDING 210 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="5" FT Condition: D FT BINDING 50 FT /ligand="substrate" FT Condition: [HD] FT BINDING 101 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: Y FT BINDING 142 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: [RK] FT BINDING 209 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: [ST] FT BINDING 260 FT /ligand="substrate" FT Condition: [ED] FT BINDING 303 FT /ligand="substrate" FT Condition: [WYF] XX Size: 286-352; Related: None; Template: O67883; P55881; P0AGG0; A3MTW6; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.10 2023/06/01 //