Annotation rule MF_00097
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General rule information [?]

Accession MF_00097
Dates 1-JUN-2001 (Created)
10-OCT-2014 (Last updated, Version 41)
Name TMP_synthase
Scope Bacteria; except Cyanobacteria
Templates P39594 (THIE_BACSU); P30137 (THIE_ECOLI); P9WG75 (THIE_MYCTU): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=Thiamine-phosphate synthase;
Short=TP synthase;
AltName: Full=Thiamine-phosphate pyrophosphorylase;
Short=TMP pyrophosphorylase;
Gene name

Comments [?]

Function Condenses 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 2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate.
case <FT:4> or <FT:5>
Cofactor Mg(2+)
Note: Binds 1 Mg(2+) ion per subunit.
end case

Keywords [?]

case <FT:4> or <FT:5>
end case

Gene Ontology [?]

GO:0000287; Molecular function: magnesium ion binding.
GO:0004789; Molecular function: thiamine-phosphate diphosphorylase activity.
GO:0009228; Biological process: thiamine biosynthetic process.

Cross-references [?]

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

Features [?]

From: THIE_BACSU (P39594)
Key     From     To       Description   Tag   Condition   FTGroup
REGION     44     48       HMP-PP binding     Q-x-R-x-[KE]  
REGION     143     145       THZ-P binding     [TS]-x-[TS]  
REGION (Optional)     195     196       THZ-P binding     [IVL]-[ST]  
METAL     80     80       Magnesium     [DE]   1
METAL     99     99       Magnesium     [DE]   1
BINDING     79     79       HMP-PP     [ND]  
BINDING     117     117       HMP-PP     [ST]  
BINDING     146     146       HMP-PP     [KH]  
BINDING     175     175       THZ-P; via amide nitrogen     [GA]  

Additional information [?]

Size range 204-240 amino acids
Related rules MF_01327 (THIE supersedes the current rule)
Fusion Nter: MF_00228 (thiM); Cter: MF_00089 (thiC), <thiD>, <Unknown>
Comments Unknown N-terminal domain in Cyanobacteria, 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 COREFCORGL, 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.