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Information on EC 2.5.1.3 - thiamine phosphate synthase and Organism(s) Bacillus subtilis and UniProt Accession P39594

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EC Tree
IUBMB Comments
The enzyme catalyses the penultimate reaction in thiamine de novo biosynthesis, condensing the pyrimidine and thiazole components. The enzyme is thought to accept the product of EC 2.8.1.10, thiazole synthase, as its substrate. However, it has been shown that in some bacteria, such as Bacillus subtilis, an additional enzyme, thiazole tautomerase (EC 5.3.99.10) converts that compound into its tautomer 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate, and that it is the latter that serves as the substrate for the synthase. In addition to this activity, the enzyme participates in a salvage pathway, acting on 4-methyl-5-(2-phosphooxyethyl)thiazole, which is produced from thiamine degradation products. In yeast this activity is found in a bifunctional enzyme (THI6) and in the plant Arabidopsis thaliana the activity is part of a trifunctional enzyme (TH1).
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Bacillus subtilis
UNIPROT: P39594
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
thin protein, thiamin phosphate synthase, tmp-ppase, tmppase, thiamine phosphate synthase, thiamine-phosphate pyrophosphorylase, thiamin-phosphate pyrophosphorylase, thiamine phosphate pyrophosphorylase, tmp pyrophosphorylase, thiamin phosphate pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-methyl-4-amino-5-hydroxymethylpyrimidinepyrophosphate:4-methyl-5-(2'-phosphoethyl)-thiazole 2-methyl-4-aminopyrimidine-5-methenyltransferase
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pyrophosphorylase, thiamin phosphate
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thiamin phosphate pyrophosphorylase
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thiamin phosphate synthase
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thiamin-phosphate pyrophosphorylase
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thiamine monophosphate pyrophosphorylase
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thiamine phosphate pyrophosphorylase
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thiamine-phosphate diphosphorylase
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thiamine-phosphate pyrophosphorylase
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thiamine-phosphate synthase
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thiaminephosphate pyrophosphorylase
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TMP pyrophosphorylase
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TMP-PPase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-amino-2-methyl-5-(diphosphomethyl)pyrimidine + 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate = diphosphate + thiamine phosphate + CO2
show the reaction diagram
dissociative SN1 mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxymethylpyrimidine group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
4-amino-2-methyl-5-diphosphomethylpyrimidine:2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate 4-amino-2-methylpyrimidine-5-methenyltransferase (decarboxylating)
The enzyme catalyses the penultimate reaction in thiamine de novo biosynthesis, condensing the pyrimidine and thiazole components. The enzyme is thought to accept the product of EC 2.8.1.10, thiazole synthase, as its substrate. However, it has been shown that in some bacteria, such as Bacillus subtilis, an additional enzyme, thiazole tautomerase (EC 5.3.99.10) converts that compound into its tautomer 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate, and that it is the latter that serves as the substrate for the synthase. In addition to this activity, the enzyme participates in a salvage pathway, acting on 4-methyl-5-(2-phosphooxyethyl)thiazole, which is produced from thiamine degradation products. In yeast this activity is found in a bifunctional enzyme (THI6) and in the plant Arabidopsis thaliana the activity is part of a trifunctional enzyme (TH1).
CAS REGISTRY NUMBER
COMMENTARY hide
9030-30-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + (R,Z)-2-(2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate
diphosphate + thiamine phosphate + CO2
show the reaction diagram
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the enzyme catalyzes the tautomerization and decarboxylation of the intermediate (2R,5Z)-3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-carboxy-4-methyl-5-[2-(phosphonooxy)ethylidene]-2,5-dihydro-1,3-thiazol-3-ium
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?
2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate
diphosphate + thiamine phosphate + CO2
show the reaction diagram
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the enzyme catalyzes the decarboxylation of the intermediate 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-carboxy-4-methyl-5-[2-(phosphonooxy)ethyl]-1,3-thiazol-3-ium
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?
2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)-thiazole
thiamine monophosphate + diphosphate
show the reaction diagram
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?
2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)-thiazole
thiamine monophosphate + diphosphate
show the reaction diagram
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?
4-amino-5-(hydroxymethyl)-2-(trifluoromethyl)pyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)-thiazole
?
show the reaction diagram
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poor substrate
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4-amino-5-(hydroxymethyl)-2-methoxypyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)-thiazole
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show the reaction diagram
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good substrate
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + (R,Z)-2-(2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate
diphosphate + thiamine phosphate + CO2
show the reaction diagram
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the enzyme catalyzes the tautomerization and decarboxylation of the intermediate (2R,5Z)-3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-carboxy-4-methyl-5-[2-(phosphonooxy)ethylidene]-2,5-dihydro-1,3-thiazol-3-ium
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?
2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate
diphosphate + thiamine phosphate + CO2
show the reaction diagram
-
the enzyme catalyzes the decarboxylation of the intermediate 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-carboxy-4-methyl-5-[2-(phosphonooxy)ethyl]-1,3-thiazol-3-ium
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?
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion, crystal structure at 1.25 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from E. coli overexpression strain
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reddick, J.J.; Nicewonger, R.; Begley, T.P.
Mechanistic studies on thiamin phosphate synthase: evidence for a dissociative mechanism
Biochemistry
40
10095-10102
2001
Bacillus subtilis
Manually annotated by BRENDA team
Chiu, H.J.; Reddick, J.J.; Begley, T.P.; Ealick, S.E.
Crystal structure of thiamin phosphate synthase from Bacillus subtilis at 1.25 A resolution
Biochemistry
38
6460-6470
1999
Bacillus subtilis (P39594), Bacillus subtilis
Manually annotated by BRENDA team
Hazra, A.B.; Han, Y.; Chatterjee, A.; Zhang, Y.; Lai, R.Y.; Ealick, S.E.; Begley, T.P.
A missing enzyme in thiamin thiazole biosynthesis: identification of TenI as a thiazole tautomerase
J. Am. Chem. Soc.
133
9311-9319
2011
Bacillus subtilis (P39594), Bacillus subtilis 168 (P39594)
Manually annotated by BRENDA team