Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.5.1.3 - thiamine phosphate synthase

for references in articles please use BRENDA:EC2.5.1.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: Q97VS8
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
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, thiamine phosphate pyrophosphorylase, thiamin-phosphate pyrophosphorylase, tmp pyrophosphorylase, thiamin phosphate pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
thiamin phosphate synthase
-
2-methyl-4-amino-5-hydroxymethylpyrimidinepyrophosphate:4-methyl-5-(2'-phosphoethyl)-thiazole 2-methyl-4-aminopyrimidine-5-methenyltransferase
-
-
-
-
pyrophosphorylase, thiamin phosphate
-
-
-
-
thiamin phosphate pyrophosphorylase
-
-
-
-
thiamin phosphate synthase
-
-
-
-
thiamin-phosphate pyrophosphorylase
-
-
-
-
thiamine monophosphate pyrophosphorylase
-
-
-
-
thiamine phosphate pyrophosphorylase
-
-
-
-
thiamine-phosphate diphosphorylase
-
-
-
-
thiamine-phosphate pyrophosphorylase
-
-
-
-
thiamine-phosphate synthase
-
-
-
-
thiaminephosphate pyrophosphorylase
-
-
-
-
TMP pyrophosphorylase
-
-
-
-
TMP-PPase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxymethylpyrimidine group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q97VS8_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
137
0
15575
TrEMBL
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of YjbQ complements the thiamin auxotrophy of the Escherichia coli MC1061DELTAthiE strain, in spite of their thiamine phosphate synthase activity being several orders of magnitude lower than that of the thiE-coded enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morett, E.; Saab-Rincon, G.; Olvera, L.; Olvera, M.; Flores, H.; Grande, R.
Sensitive genome-wide screen for low secondary enzymatic activities: the YjbQ family shows thiamin phosphate synthase activity
J. Mol. Biol.
376
839-853
2008
Escherichia coli, Pyrococcus furiosus (Q8U3C6), Saccharolobus solfataricus (Q97VS8), Thermotoga maritima (Q9WZI2), Thermotoga maritima (Q9X2I5), Saccharolobus solfataricus P2 (Q97VS8), Thermotoga maritima DSM 3109 (Q9WZI2), Thermotoga maritima DSM 3109 (Q9X2I5)
Manually annotated by BRENDA team