TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
1-243
2.46e-165
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.
The actual alignment was detected with superfamily member CHL00162:
Pssm-ID: 473867 Cd Length: 267 Bit Score: 458.02 E-value: 2.46e-165
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ...
4-242
5.93e-136
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH).
Pssm-ID: 240079 Cd Length: 248 Bit Score: 382.61 E-value: 5.93e-136
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ...
1-242
2.59e-134
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and metabolism]; Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 441625 Cd Length: 259 Bit Score: 378.99 E-value: 2.59e-134
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
9-242
1.35e-116
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS.
Pssm-ID: 428589 Cd Length: 247 Bit Score: 333.83 E-value: 1.35e-116
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ...
4-242
5.93e-136
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH).
Pssm-ID: 240079 Cd Length: 248 Bit Score: 382.61 E-value: 5.93e-136
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ...
1-242
2.59e-134
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and metabolism]; Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 441625 Cd Length: 259 Bit Score: 378.99 E-value: 2.59e-134
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
9-242
1.35e-116
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS.
Pssm-ID: 428589 Cd Length: 247 Bit Score: 333.83 E-value: 1.35e-116
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
172-229
7.62e-06
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.
Pssm-ID: 240078 Cd Length: 283 Bit Score: 46.09 E-value: 7.62e-06
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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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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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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Domains are color coded according to superfamilies
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Others (non-specific hits) and
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if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
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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,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
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
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
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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