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Literature summary extracted from

  • Hwang, S.; Cordova, B.; Abdo, M.; Pfeiffer, F.; Maupin-Furlow, J.-A.
    ThiN as a versatile domain of transcriptional repressors and catalytic enzymes of thiamine biosynthesis (2017), J. Bacteriol., 199, pii: e00810-16 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.17 gene thiC, archaeal ThiC is encoded by leaderless transcripts, ruling out a riboswitch mechanism. Instead, transcription factor ThiR, that harbors an N-terminal helix-turn-helix (HTH) DNA binding domain and C-terminal ThiN (TMP synthase) domain, is identified. In the presence of thiamine, ThiR represses the expression of thiC by a DNA operator sequence that is conserved across archaeal phyla. Sequence comparisons and genetic organization analysis Haloferax volcanii

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 Haloferax volcanii
-
 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?
4.1.99.17 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine Haloferax volcanii ATCC 29605
-
 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.17 Haloferax volcanii D4GV87
-
-
4.1.99.17 Haloferax volcanii ATCC 29605 D4GV87
-
-

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
-
 Haloferax volcanii 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?
4.1.99.17 5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
-
 Haloferax volcanii ATCC 29605 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.99.17 2-methyl-4-amino-5-hydroxymethylpyrimidine phosphate synthase
-
 Haloferax volcanii
4.1.99.17 HMP phosphate synthase
-
 Haloferax volcanii
4.1.99.17 HMP-P synthase
-
 Haloferax volcanii
4.1.99.17 thiC
-
 Haloferax volcanii

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.17 S-adenosyl-L-methionine
-
 Haloferax volcanii

Expression

EC Number Organism Comment Expression
4.1.99.17 Haloferax volcanii transcription factor ThiR, that harbors an N-terminal helix-turn-helix (HTH) DNA binding domain and C-terminal ThiN (TMP synthase) domain, represses the expression of thiC in presence of thiamine by a DNA operator sequence that is conserved across archaeal phyla. Despite having a ThiN domain, ThiR is catalytically inactive in compensating for the loss of ThiE (TMP synthase) function. ThiR homologs are widespread in archaea, suggesting that the regulation of these thiamine biosynthesis genes is governed by a repressor protein and not by a riboswitch or activation mechanism down

General Information

EC Number General Information Comment Organism
4.1.99.17 malfunction a DELTAthiC mutant displays thiamine auxotrophy, the phenotype is not due to polar mutations, as the strain is restored to wild-type growth by the expression of the corresponding thiC gene in trans Haloferax volcanii
4.1.99.17 metabolism in the archaeon Haloferax volcanii, thiamine biosynthesis is carried out by a chimera of the eukaryote-like THI4 pathway to synthesize the thiazole ring with a bacterial ThiC-like pathway to synthesize the pyrimidine (HMP) moiety. The enzyme ThiC is involved in thiamine biosynthesis. Haloferax volcanii uses a eukaryote-like Thi4 (thiamine thiazole synthase) for the production of the thiazole ring and condenses this ring with a pyrimidine moiety synthesized by an apparent bacterium-like ThiC (2-methyl-4-amino-5-hydroxymethylpyrimidine [HMP] phosphate synthase) branch. In the presence of thiamine, transcription factor ThiR represses the expression of thiC by a DNA operator sequence. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch. In archaea, thiamine biosynthesis is an apparent chimera of eukaryote- and bacterium-type pathways Haloferax volcanii
4.1.99.17 physiological function the enzyme ThiC is involved in thiamine biosynthesis. The archaeon Haloferax volcanii uses a eukaryote-like Thi4 (thiamine thiazole synthase) for the production of the thiazole ring and condenses this ring with a pyrimidine moiety synthesized by an apparent bacterium-like ThiC (2-methyl-4-amino-5-hydroxymethylpyrimidine [HMP] phosphate synthase) branch. In the presence of thiamine, transcription factor ThiR represses the expression of thiC by a DNA operator sequence. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch, mechanims, overview Haloferax volcanii