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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-[sulfur-carrier protein ThiS] = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-[sulfur-carrier protein ThiS] = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-[sulfur-carrier protein ThiS] = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
final step of the thiamin-thiazole biosynthesis is the concersion of a labile adenylated thiazole tautomer to the adenylated thiazole product. The conversion has an absolute requirement for enzyme catalysis
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-[sulfur-carrier protein ThiS] = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
mechanism involves the generation of a ketone at C3 of 1-deoxy-D-xylulose-5-phosphate by an Amadori-type rearrangement of the imine followed by nucleophillic addition of the sulfur carrier protein to this carbonyl group
1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-[sulfur-carrier protein ThiS] = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
the cofactor nicotinamide adenine dinucleotide is converted into adenosine diphospho-5-(beta-ethyl)-4-methylthiazole-2-carboxylic acid. The ADT ligand is tightly bound and can be released in vitro only upon protein denaturation. In this mechanism, cleavage of the N-glycosyl bond of NAD gives ADP-ribose.The first step in thiazole formation is similar to the chemistry used in ADP ribosylation
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
additional information
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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product is a dearomatized thiazole tautomer, not thiazole phosphate
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
ThiG alone can catalyze the formation of thiazole phosphate
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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additional information
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the in vitro thiazole synthase activity of cleared lysates or desalted proteins is dependent upon the addition of purified ThiG/ThiH-His complex, tyrosine, and an as yet unidentified intermediate present in the protein fraction from the cells
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additional information
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the thiazole-forming activity requires four proteins isolated as heterodimers: ThiGH and ThiFS. Reconstitution of the [4Fe-4S] cluster in ThiH is essential for activity, as is the use of ThiS in the thiocarboxylate form. S-adenosylmethionine binds to the [4Fe-4S] cluster, which becomes more susceptible to reduction to the +1 state. In addition to the proteins, 1-deoxy-xylulose-5-phosphate, tyrosine, S-adenosylmethionine, and a reductant are required. 1 mol equivalent of thiazole phosphate is formed per ThiGH. For each mole of thiazole phosphate formed, 1 equivalent of S-adenosylmethionine and 1 equivalent of tyrosine are utilized, and 1 equivalent of 5-deoxyadenosine is produced. Mechanistic hypothesis suggests that S-adensylmethionine is reductively cleaved to yield a highly reactive 5-deoxyadenosyl radical. This radical abstracts the phenolic hydrogen atom from tyrosine, and the resultant substrate radical cleaves to yield dehydroglycine, which is required by ThiG for the thiazole cyclization reaction
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additional information
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the thiazole-forming activity requires four proteins isolated as heterodimers: ThiGH and ThiFS. Reconstitution of the [4Fe-4S] cluster in ThiH is essential for activity, as is the use of ThiS in the thiocarboxylate form. S-adenosylmethionine binds to the [4Fe-4S] cluster, which becomes more susceptible to reduction to the +1 state. In addition to the proteins, 1-deoxy-xylulose-5-phosphate, tyrosine, S-adenosylmethionine, and a reductant are required. 1 mol equivalent of thiazole phosphate is formed per ThiGH. For each mole of thiazole phosphate formed, 1 equivalent of S-adenosylmethionine and 1 equivalent of tyrosine are utilized, and 1 equivalent of 5-deoxyadenosine is produced. Mechanistic hypothesis suggests that S-adensylmethionine is reductively cleaved to yield a highly reactive 5-deoxyadenosyl radical. This radical abstracts the phenolic hydrogen atom from tyrosine, and the resultant substrate radical cleaves to yield dehydroglycine, which is required by ThiG for the thiazole cyclization reaction
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THI4 is a suicide enzyme serving as a cosubstrate rather than an enzyme for the formation of the thiazole moiety of thiamine. This assembly involves a complex reaction sequence in which NAD serves as the source of the five-carbon chain and THI4 serves as the sulfur source
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additional information
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THI4 is a suicide enzyme serving as a cosubstrate rather than an enzyme for the formation of the thiazole moiety of thiamine. This assembly involves a complex reaction sequence in which NAD serves as the source of the five-carbon chain and THI4 serves as the sulfur source
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS]
2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O
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metabolism
the enzyme is involved in thiamin biosynthesis. The enzyme is involved in catalysis of rearrangement of 1-deoxy-D-xylulose 5-phosphate to produce the thiazole phosphate moiety of thiamine
malfunction
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the enzyme deletion mutant displays impaired virulence and growth in thiamine-free medium but maintains its normal growth rate in the rice tissues
malfunction
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the enzyme deletion mutant displays impaired virulence and growth in thiamine-free medium but maintains its normal growth rate in the rice tissues
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physiological function
biochemical function of each of the proteins involved in biosynthesis of thiamin diphosphate is as follws: ThiF catalyzes the adenylation of ThiS, NifS catalyzes the transfer of sulfur from cysteine to the acyl adenylate of ThiS, ThiO catalyzes the oxidation of glycine to the corresponding imine, and ThiG catalyzes the formation of the thiazole phosphate ring
physiological function
reaction product of ThiG is a thiazole tautomer (R,Z)-2-(2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate, which is aromatized by tautomerase TenI to yield 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate
physiological function
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the enzyme is involved in abscisic acid-regulated stomatal movement, S-type anion channels, and the plant's drought response. The enzyme interacts with and represses Ca2+-dependent protein kinase CPK33 activity
physiological function
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the enzyme is involved in Xanthomonas oryzae virulence in rice by preventing cell aggregation
physiological function
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the enzyme is involved in Xanthomonas oryzae virulence in rice by preventing cell aggregation
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structure of ThiG in complex with ThiS, the sulfur carrier protein, at 3.15 A resolution. Thiazole synthase is a tetramer with 222 symmetry. The monomer is a (betaalpha)8 barrel with similarities to the aldolase class 1 and flavin mononucleotide dependent oxidoreductase and phosphate binding superfamilies. The sulfur carrier protein ThiS is a compact protein with a fold similar to that of ubiquitin. Modeling the substrate, deoxy-D-xylulose 5-phosphate in the active site identifies Glu98 and Asp182 as active site residues likely to be involved in the catalysis of thiazole formation
wild type enzyme complexed with ADP-ribulose, hanging drop vapor diffusion method, using 1.05 M potassium/sodium tartrate, 0.1 M CHES/sodium hydroxide, pH 9.5 and 0.2 M lithium sulfate
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wild type enzyme with bound glycine imine intermediate and iron, hanging drop vapor diffusion method, using 1.0 M sodium citrate, 0.1 M CHES/sodium hydroxide, pH 9.5
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C205S variant with a bound glycine imine intermediate, hanging drop vapor diffusion method, using 25% (w/v) PEG1500, 0.0125 M succinic acid, 0.044 M sodium dihydrogen phosphate, and 0.044 M glycine, pH 8.5
native protein to 1.8 A resolution. Thi4 exists as an homooctamer with the disordered and largely hydrophilic N-terminal regions located on the exterior of the molecule. The octamer has the shape of a ring with flattened sides. Adenosine diphospho-5-(beta-ethyl)-4-methylthiazole-2-carboxylic acid is bound to the Thi4 active site, which is located near the inner ring of the octameric complex.. NAD is the most likely precursor
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Park, J.H.; Dorrestein, P.C.; Zhai, H.; Kinsland, C.; McLafferty, F.W.; Begley, T.P.
Biosynthesis of the thiazole moiety of thiamin pyrophosphate (vitamin B1)
Biochemistry
42
12430-12438
2003
Bacillus subtilis (O31618)
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Settembre, E.C.; Dorrestein, P.C.; Zhai, H.; Chatterjee, A.; McLafferty, F.W.; Begley, T.P.; Ealick, S.E.
Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex
Biochemistry
43
11647-11657
2004
Bacillus subtilis (O31618), Bacillus subtilis
brenda
Hazra, A.; Chatterjee, A.; Begley, T.P.
Biosynthesis of the thiamin thiazole in Bacillus subtilis: identification of the product of the thiazole synthase-catalyzed reaction
J. Am. Chem. Soc.
131
3225-3229
2009
Bacillus subtilis (O31618), Bacillus subtilis
brenda
Jurgenson, C.T.; Chatterjee, A.; Begley, T.P.; Ealick, S.E.
Structural insights into the function of the thiamin biosynthetic enzyme Thi4 from Saccharomyces cerevisiae
Biochemistry
45
11061-11070
2006
Saccharomyces cerevisiae (P32318), Saccharomyces cerevisiae
brenda
Dorrestein, P.C.; Zhai, H.; Taylor, S.V.; McLafferty, F.W.; Begley, T.P.
The biosynthesis of the thiazole phosphate moiety of thiamin (vitamin B1): the early steps catalyzed by thiazole synthase
J. Am. Chem. Soc.
126
3091-3096
2004
Bacillus subtilis (O31618), Bacillus subtilis
brenda
Chatterjee, A.; Schroeder, F.C.; Jurgenson, C.T.; Ealick, S.E.; Begley, T.P.
Biosynthesis of the thiamin-thiazole in eukaryotes: identification of a thiazole tautomer intermediate
J. Am. Chem. Soc.
130
11394-11398
2008
Saccharomyces cerevisiae
brenda
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 (O31618)
brenda
Leonardi, R.; Roach, P.L.
Thiamine biosynthesis in Escherichia coli: in vitro reconstitution of the thiazole synthase activity
J. Biol. Chem.
279
17054-17062
2004
Escherichia coli
brenda
Kriek, M.; Martins, F.; Leonardi, R.; Fairhurst, S.A.; Lowe, D.J.; Roach, P.L.
Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro
J. Biol. Chem.
282
17413-17423
2007
Escherichia coli (P30139), Escherichia coli
brenda
Chatterjee, A.; Abeydeera, N.D.; Bale, S.; Pai, P.J.; Dorrestein, P.C.; Russell, D.H.; Ealick, S.E.; Begley, T.P.
Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase
Nature
478
542-546
2011
Saccharomyces cerevisiae (P32318), Saccharomyces cerevisiae
brenda
Rohini, K.; Srikumar, P.S.
Structural insights on Mycobacterium tuberculosis thiazole synthase-a molecular dynamics/docking approach
Appl. Biochem. Biotechnol.
169
1790-1798
2013
Mycobacterium tuberculosis (A5TZE3), Mycobacterium tuberculosis
brenda
Zhang, X.; Eser, B.E.; Chanani, P.K.; Begley, T.P.; Ealick, S.E.
Structural Basis for iron-mediated sulfur transfer in archael and yeast thiazole synthases
Biochemistry
55
1826-1838
2016
Methanocaldococcus jannaschii, Methanotorris igneus, Saccharomyces cerevisiae (P32318)
brenda
Li, C.L.; Wang, M.; Wu, X.M.; Chen, D.H.; Lv, H.J.; Shen, J.L.; Qiao, Z.; Zhang, W.
THI1, a thiamine thiazole synthase, interacts with Ca2+-dependent protein kinase CPK33 and modulates the S-type anion channels and stomatal closure in Arabidopsis
Plant Physiol.
170
1090-1104
2016
Arabidopsis thaliana
brenda
Yu, X.; Liang, X.; Liu, K.; Dong, W.; Wang, J.; Zhou, M.G.
The thiG gene is required for full virulence of Xanthomonas oryzae pv. oryzae by preventing cell aggregation
PLoS ONE
10
e0134237
2015
Xanthomonas oryzae pv. oryzae, Xanthomonas oryzae pv. oryzae ZJ173
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