Information on EC 2.8.1.10 - thiazole synthase

for references in articles please use BRENDA:EC2.8.1.10
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.8.1.10
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RECOMMENDED NAME
GeneOntology No.
thiazole synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
thiazole biosynthesis I (facultative anaerobic bacteria)
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thiazole biosynthesis II (aerobic bacteria)
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vitamin B1 metabolism
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Thiamine metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
1-deoxy-D-xylulose 5-phosphate:thiol sulfurtransferase
H2S can provide the sulfur in vitro. Part of the pathway for thiamine biosynthesis.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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strong stimulation
S-adenosylmethionine
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strong stimulation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34991
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x * 34991, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 34991, calculated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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
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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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and glutathione Sepharose column chromatography
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Ni-NTA column chromatography and Superdex 200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D182A
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no residual activity
E98A
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less than 3% residual activity
additional information
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overexpression of His-tagged proteins ThiF, NifS, ThiO, and ThiSG Escherichia coli BL21and incubation with L-cysteine in the presence of dithiothreitol and ATP to form ThiS-COSH. This is then added to 1-deoxy-D-xylulose 5-phosphate and glycine in the presence of ThiO and ThiG to produce the product of the thiazole synthase-catalyzed reaction. Reaction product is a dearomatized thiazole tautomer
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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synthesis of the thiazole moiety of thiamin from glycine, cysteine, and deoxy-D-xylulose-5-phosphate using overexpressed Bacillus subtilis ThiF, ThiS, ThiO, ThiG, and a NifS-like protein
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