AC MF_01327; DC Protein; auto TR HAMAP; MF_01327; -; 1; level=0 XX Names: TMP_synthase_cyanobact XX ID THIE DE RecName: Full=Thiamine-phosphate synthase; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiE; XX CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). CC -!- CATALYTIC ACTIVITY: CC Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl CC phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 CC H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2- CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate CC + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, CC ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl- CC 5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine CC phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, CC ChEBI:CHEBI:58296; EC=2.5.1.3; case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; end case CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine CC and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. XX DR Pfam; PF02581; TMP-TENI; 1; trigger=no DR NCBIfam; TIGR00693; ThiE; 1; trigger=no DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1; trigger=no XX KW Thiamine biosynthesis KW Transferase case KW Magnesium KW Metal-binding end case XX GO GO:0000287; F:magnesium ion binding GO GO:0004789; F:thiamine-phosphate diphosphorylase activity GO GO:0009228; P:thiamine biosynthetic process XX FT From: THIE_NOSS1 (Q8YX72) FT REGION Nter..129 FT /note="Unknown" FT REGION 130..Cter FT /note="Thiamine-phosphate synthase" FT BINDING 177..181 FT /ligand="4-amino-2-methyl-5- FT (diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT Condition: Q-x-R-x-K FT BINDING 274..276 FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- FT ylidene]ethyl phosphate" FT /ligand_id="ChEBI:CHEBI:62899" FT Optional; Condition: T-x-T FT BINDING 210 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: [DN] FT BINDING 229 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: [DE] FT BINDING 209 FT /ligand="4-amino-2-methyl-5- FT (diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT Condition: N FT BINDING 248 FT /ligand="4-amino-2-methyl-5- FT (diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT Condition: S FT BINDING 277 FT /ligand="4-amino-2-methyl-5- FT (diphosphooxymethyl)pyrimidine" FT /ligand_id="ChEBI:CHEBI:57841" FT Condition: K FT BINDING 304 FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- FT ylidene]ethyl phosphate" FT /ligand_id="ChEBI:CHEBI:62899" FT Condition: G XX Size: 341-353; Related: MF_00097; Template: Q8YX72; Scope: Bacteria; Cyanobacteriota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: Unknown N-terminal domain in Cyanobacteriota. All other bacteria without this domain belong to family MF_00097. XX # Revision 1.33 2023/06/01 //