phosphomethylpyrimidine synthase ThiC catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction
4-amino-2-methyl-5-hydroxymethylpyrimidine (HMP) synthase ThiC [Coenzyme transport and ...
3-429
0e+00
4-amino-2-methyl-5-hydroxymethylpyrimidine (HMP) synthase ThiC [Coenzyme transport and metabolism]; 4-amino-2-methyl-5-hydroxymethylpyrimidine (HMP) synthase ThiC is part of the Pathway/BioSystem: Thiamine biosynthesis
:
Pssm-ID: 440191 Cd Length: 430 Bit Score: 778.46 E-value: 0e+00
4-amino-2-methyl-5-hydroxymethylpyrimidine (HMP) synthase ThiC [Coenzyme transport and ...
3-429
0e+00
4-amino-2-methyl-5-hydroxymethylpyrimidine (HMP) synthase ThiC [Coenzyme transport and metabolism]; 4-amino-2-methyl-5-hydroxymethylpyrimidine (HMP) synthase ThiC is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440191 Cd Length: 430 Bit Score: 778.46 E-value: 0e+00
Radical SAM ThiC family; ThiC is found within the thiamine biosynthesis operon. ThiC is ...
5-423
0e+00
Radical SAM ThiC family; ThiC is found within the thiamine biosynthesis operon. ThiC is involved in pyrimidine biosynthesis. ThiC participates in the formation of 4-Amino-5-hydroxymethyl-2-methylpyrimidine from AIR, an intermediate in the de novo pyrimidine biosynthesis. Thic is a member of the radical SAM superfamily.
Pssm-ID: 460397 Cd Length: 420 Bit Score: 773.87 E-value: 0e+00
phosphomethylpyrimidine synthase; The thiC ortholog is designated thiA in Bacillus subtilis. ...
5-425
0e+00
phosphomethylpyrimidine synthase; The thiC ortholog is designated thiA in Bacillus subtilis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 129294 Cd Length: 423 Bit Score: 558.21 E-value: 0e+00
4-amino-2-methyl-5-hydroxymethylpyrimidine (HMP) synthase ThiC [Coenzyme transport and ...
3-429
0e+00
4-amino-2-methyl-5-hydroxymethylpyrimidine (HMP) synthase ThiC [Coenzyme transport and metabolism]; 4-amino-2-methyl-5-hydroxymethylpyrimidine (HMP) synthase ThiC is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440191 Cd Length: 430 Bit Score: 778.46 E-value: 0e+00
Radical SAM ThiC family; ThiC is found within the thiamine biosynthesis operon. ThiC is ...
5-423
0e+00
Radical SAM ThiC family; ThiC is found within the thiamine biosynthesis operon. ThiC is involved in pyrimidine biosynthesis. ThiC participates in the formation of 4-Amino-5-hydroxymethyl-2-methylpyrimidine from AIR, an intermediate in the de novo pyrimidine biosynthesis. Thic is a member of the radical SAM superfamily.
Pssm-ID: 460397 Cd Length: 420 Bit Score: 773.87 E-value: 0e+00
phosphomethylpyrimidine synthase; The thiC ortholog is designated thiA in Bacillus subtilis. ...
5-425
0e+00
phosphomethylpyrimidine synthase; The thiC ortholog is designated thiA in Bacillus subtilis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 129294 Cd Length: 423 Bit Score: 558.21 E-value: 0e+00
ThiC-like protein 1; Members of this protein family closely resemble ThiC, an enzyme that ...
5-425
2.16e-176
ThiC-like protein 1; Members of this protein family closely resemble ThiC, an enzyme that performs a complex rearrangement during thiamin biosynthesis, but instead occur as one of two adjacent additional paralogs to bona fide ThiC, in a conserved gene neighborhood with a pair of B12 binding domain/radical SAM domain proteins. Members of the ThiC family are non-canonical radical SAM enzymes, using a C-terminal Cys-rich motif to ligand a 4Fe-4S cluster that cleaves S-adenosylmethionine (SAM), but that sequence region does not belong to pfam04055.
Pssm-ID: 275179 Cd Length: 426 Bit Score: 499.68 E-value: 2.16e-176
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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