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Literature summary extracted from

  • Zhang, Q.; Liu, W.
    Complex biotransformations catalyzed by radical S-adenosylmethionine enzymes (2011), J. Biol. Chem., 286, 30245-30252.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.99.17 Fe2+ the enzyme contains a [4Fe-4S] cluster bound by the CXXCXXXXC motif Caulobacter vibrioides
4.1.99.17 Fe2+ the enzyme contains a [4Fe-4S] cluster bound by the CXXCXXXXC motif Salmonella enterica

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.17 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine Caulobacter vibrioides
-
 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?
4.1.99.17 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine Salmonella enterica
-
 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.17 Caulobacter vibrioides Q9A6Q5 gene thiC
-
4.1.99.17 Salmonella enterica Q9L9I7 subsp. enterica, serovar Typhimurium LT2, gene thiC
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.99.17 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO radical reaction mechanism, overview Caulobacter vibrioides
a
4.1.99.17 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO radical reaction mechanism, overview Salmonella enterica
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.17 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
-
 Caulobacter vibrioides 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?
4.1.99.17 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
-
 Salmonella enterica 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?
4.1.99.17 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine optimal assay condition is set both by using flavodoxin, flavodoxin reductase, and NADPH to reduce the [4Fe-4S] cluster of ThiC and by obviation of the prolonged reaction time to minimize the uncoupled AdoH production Caulobacter vibrioides 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?
4.1.99.17 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine optimal assay condition is set both by using flavodoxin, flavodoxin reductase, and NADPH to reduce the [4Fe-4S] cluster of ThiC and by obviation of the prolonged reaction time to minimize the uncoupled AdoH production Salmonella enterica 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.99.17 HMP-P synthase
-
 Caulobacter vibrioides
4.1.99.17 HMP-P synthase
-
 Salmonella enterica
4.1.99.17 thiC
-
 Caulobacter vibrioides
4.1.99.17 thiC
-
 Salmonella enterica

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.17 S-adenosyl-L-methionine a S-adenosyl-L-methionine radical enzyme Caulobacter vibrioides
4.1.99.17 S-adenosyl-L-methionine a S-adenosyl-L-methionine radical enzyme Salmonella enterica

General Information

EC Number General Information Comment Organism
4.1.99.17 evolution the enzyme is a member of the radical S-adenosylmethionine (AdoMet) superfamily, reactions catalyzed by the radical AdoMet superfamily include mainly glycyl radical generation, sulfur insertion, methylation, methylthiolation, oxidation, isomerization, elimination (fragmentation), overview. ThiC does not contain the canonical CXXXCXXC motif in the N-terminal domain, as do most of the radical AdoMet enzymes, but a CXXCXXXXC motif Caulobacter vibrioides
4.1.99.17 evolution the enzyme is a member of the radical S-adenosylmethionine (AdoMet) superfamily, reactions catalyzed by the radical AdoMet superfamily include mainly glycyl radical generation, sulfur insertion, methylation, methylthiolation, oxidation, isomerization, elimination (fragmentation), overview. ThiC does not contain the canonical CXXXCXXC motif in the N-terminal domain, as do most of the radical AdoMet enzymes, but a CXXCXXXXC motif Salmonella enterica
4.1.99.17 metabolism the enzyme is important in thiamine biosynthesis, an essential compound in all living organisms that participates in several key cellular processes, such as carbohydrate and amino acid metabolism. Thiamine consists of a thiazole and a pyrimidine heterocycle, which are synthesized separately and assembled together by thiamine phosphate synthase Caulobacter vibrioides
4.1.99.17 metabolism the enzyme is important in thiamine biosynthesis, an essential compound in all living organisms that participates in several key cellular processes, such as carbohydrate and amino acid metabolism. Thiamine consists of a thiazole and a pyrimidine heterocycle, which are synthesized separately and assembled together by thiamine phosphate synthase Salmonella enterica