CaiB/BaiF CoA transferase family protein catalyzes the reversible transfer of the CoA moiety from a fatty acid CoA ester to a fatty acid acceptor, might also act as an acyl-CoA racemase
CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. ...
4-347
1.83e-92
CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. Most of these enzymes belong to two well-known enzyme families, but recent work on unusual biochemical pathways of anaerobic bacteria has revealed the existence of a third family of CoA-transferases. The members of this enzyme family differ in sequence and reaction mechanism from CoA-transferases of the other families. Currently known enzymes of the new family are a formyl-CoA: oxalate CoA-transferase, a succinyl-CoA: (R)-benzylsuccinate CoA-transferase, an (E)-cinnamoyl-CoA: (R)-phenyllactate CoA-transferase, and a butyrobetainyl-CoA: (R)-carnitine CoA-transferase. In addition, a large number of proteins of unknown or differently annotated function from Bacteria, Archaea and Eukarya apparently belong to this enzyme family. Properties and reaction mechanisms of the CoA-transferases of family III are described and compared to those of the previously known CoA-transferases.
Pssm-ID: 426810 [Multi-domain] Cd Length: 367 Bit Score: 281.80 E-value: 1.83e-92
formyl-CoA transferase; This enzyme, formyl-CoA transferase, transfers coenzyme A from ...
3-200
4.73e-34
formyl-CoA transferase; This enzyme, formyl-CoA transferase, transfers coenzyme A from formyl-CoA to oxalate. It forms a pathway, together with oxalyl-CoA decarboxylase, for oxalate degradation; decarboxylation by the latter gene regenerates formyl-CoA. The two enzymes typically are encoded by a two-gene operon. [Cellular processes, Detoxification]
Pssm-ID: 211800 Cd Length: 415 Bit Score: 130.32 E-value: 4.73e-34
CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. ...
4-347
1.83e-92
CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. Most of these enzymes belong to two well-known enzyme families, but recent work on unusual biochemical pathways of anaerobic bacteria has revealed the existence of a third family of CoA-transferases. The members of this enzyme family differ in sequence and reaction mechanism from CoA-transferases of the other families. Currently known enzymes of the new family are a formyl-CoA: oxalate CoA-transferase, a succinyl-CoA: (R)-benzylsuccinate CoA-transferase, an (E)-cinnamoyl-CoA: (R)-phenyllactate CoA-transferase, and a butyrobetainyl-CoA: (R)-carnitine CoA-transferase. In addition, a large number of proteins of unknown or differently annotated function from Bacteria, Archaea and Eukarya apparently belong to this enzyme family. Properties and reaction mechanisms of the CoA-transferases of family III are described and compared to those of the previously known CoA-transferases.
Pssm-ID: 426810 [Multi-domain] Cd Length: 367 Bit Score: 281.80 E-value: 1.83e-92
formyl-CoA transferase; This enzyme, formyl-CoA transferase, transfers coenzyme A from ...
3-200
4.73e-34
formyl-CoA transferase; This enzyme, formyl-CoA transferase, transfers coenzyme A from formyl-CoA to oxalate. It forms a pathway, together with oxalyl-CoA decarboxylase, for oxalate degradation; decarboxylation by the latter gene regenerates formyl-CoA. The two enzymes typically are encoded by a two-gene operon. [Cellular processes, Detoxification]
Pssm-ID: 211800 Cd Length: 415 Bit Score: 130.32 E-value: 4.73e-34
mesaconyl-CoA isomerase; Members of this protein family belong by homology to the family of ...
2-370
5.92e-07
mesaconyl-CoA isomerase; Members of this protein family belong by homology to the family of CoA transferases. However, the characterized member from Chloroflexus aurantiacus appears to perform an intramolecular transfer, making it an isomerase. The enzyme converts mesaconyl-C1-CoA to mesaconyl-C4-CoA as part of the bicyclic 3-hydroxyproprionate pathway for carbon fixation.
Pssm-ID: 211976 Cd Length: 403 Bit Score: 51.12 E-value: 5.92e-07
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.
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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,
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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
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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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