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HAMAP rule MF_00097

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General rule information [?]

Accession MF_00097
Dates 1-JUN-2001 (Created)
1-MAR-2024 (Last updated, Version 50)
Name TMP_synthase
Scope(s) Bacteria
Archaea
Template(s) P39594 (THIE_BACSU); P30137 (THIE_ECOLI); P9WG75 (THIE_MYCTU); [ Recover all ]
Triggered by HAMAP; MF_00097 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier THIE
Protein name RecName: Full=Thiamine-phosphate synthase;
                 Short=TP synthase;
                 Short=TPS;
                 EC=2.5.1.3;
AltName: Full=Thiamine-phosphate pyrophosphorylase;
                 Short=TMP pyrophosphorylase;
                 Short=TMP-PPase;
Gene name Name=thiE;

Comments [?]

FUNCTIONCondenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
CATALYTIC ACTIVITY Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3;
CATALYTIC ACTIVITY Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2- methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3;
CATALYTIC ACTIVITY Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl- 5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:58296; EC=2.5.1.3;
case <FT:4> or <FT:5>
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.;
end case
PATHWAYCofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
SIMILARITYBelongs to the thiamine-phosphate synthase family.

Keywords [?]

Thiamine biosynthesis
Transferase
case <FT:4> or <FT:5>
Magnesium
Metal-binding
end case

Gene Ontology [?]

GO:0000287; Molecular function:magnesium ion binding
GO:0004789; Molecular function:thiamine-phosphate diphosphorylase activity
GO:0009229; Biological process:thiamine diphosphate biosynthetic process

Cross-references [?]

Pfam PF02581; TMP-TENI; 1;
NCBIfam TIGR00693; ThiE; 1;

Features [?]

From: THIE_BACSU (P39594)
Key From To Description Tag Condition FTGroup
BINDING 44 48 /ligand="4-amino-2-methyl-5- (diphosphooxymethyl)pyrimidine"
/ligand_id="ChEBI:CHEBI:57841"		 Q-x-R-x-[KE]
BINDING 143 145 /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- ylidene]ethyl phosphate"
/ligand_id="ChEBI:CHEBI:62899"		 [TS]-x-[TS]
BINDING 195 196 /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- ylidene]ethyl phosphate"
/ligand_id="ChEBI:CHEBI:62899"		 [IVL]-[ST]
BINDING 80 80 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 [DE] 1
BINDING 99 99 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 [DE] 1
BINDING 79 79 /ligand="4-amino-2-methyl-5- (diphosphooxymethyl)pyrimidine"
/ligand_id="ChEBI:CHEBI:57841"		 [ND]
BINDING 117 117 /ligand="4-amino-2-methyl-5- (diphosphooxymethyl)pyrimidine"
/ligand_id="ChEBI:CHEBI:57841"		 [ST]
BINDING 146 146 /ligand="4-amino-2-methyl-5- (diphosphooxymethyl)pyrimidine"
/ligand_id="ChEBI:CHEBI:57841"		 [KH]
BINDING 175 175 /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)- ylidene]ethyl phosphate"
/ligand_id="ChEBI:CHEBI:62899"		 [GA]

Additional information [?]

Size range 204-240 amino acids
Related rules MF_01327
Fusion Nter: MF_00228 (thiM) Cter: MF_00089 (thiC); <thiD>; <Unknown>
Comments Unknown N-terminal domain in Cyanobacteriota, this has now been put into a separate family, MF_01327. There is a second copy of ThiE in AQUAE (AQ_1366) and in GEOSL (GSU0587) that lacks the second magnesium binding site. Fusion with ThiC in BIFLO, with ThiD and an unknown domain in COREF, CORGL, with ThiD in one copy in GEOSL, with ThiM in SYMTH. There is a ThiE-like protein in BACSU: TenI, which has a different activity.



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