AC   MF_00097;
DC   Protein; auto
TR   HAMAP; MF_00097; -; 1; level=0
XX
Names: TMP_synthase
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 <FT:4> or <FT:5>
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
XX
KW   Thiamine biosynthesis
KW   Transferase
case <FT:4> or <FT:5>
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_BACSU (P39594)
FT   BINDING         44..48
FT                   /ligand="4-amino-2-methyl-5-
FT                   (diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT   Condition: Q-x-R-x-[KE]
FT   BINDING         143..145
FT                   /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT                   ylidene]ethyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:62899"
FT   Condition: [TS]-x-[TS]
FT   BINDING         195..196
FT                   /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT                   ylidene]ethyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:62899"
FT   Optional; Condition: [IVL]-[ST]
FT   BINDING         80
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: [DE]
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: [DE]
FT   BINDING         79
FT                   /ligand="4-amino-2-methyl-5-
FT                   (diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT   Condition: [ND]
FT   BINDING         117
FT                   /ligand="4-amino-2-methyl-5-
FT                   (diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT   Condition: [ST]
FT   BINDING         146
FT                   /ligand="4-amino-2-methyl-5-
FT                   (diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT   Condition: [KH]
FT   BINDING         175
FT                   /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT                   ylidene]ethyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:62899"
FT   Condition: [GA]
XX
Size: 204-240;
Related: MF_01327!;
Template: P39594; P30137; P9WG75;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: MF_00228 (thiM)
 Cter: MF_00089 (thiC); <thiD>; <Unknown>
Duplicate: in AQUAE, COREF, GEOSL, STRPN, STRR6
Plasmid: in RHIET
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.
XX
# Revision 1.49 2023/06/01
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