acetyl-CoA hydrolase/transferase family protein such as Clostridium kluyveri succinyl-CoA:coenzyme A transferase, which catalyzes the formation of succinyl-CoA from succinate and acetyl-CoA, and Escherichia coli propionyl-CoA:succinate CoA transferase, which catalyzes the transfer of coenzyme A from propionyl-CoA to succinate
succinate CoA transferase; This family of CoA transferases includes enzymes catalyzing at ...
14-493
0e+00
succinate CoA transferase; This family of CoA transferases includes enzymes catalyzing at least two related but distinct activities. The E. coli YgfH protein has been characterized as a propionyl-CoA:succinate CoA transferase where it appears to be involved in a pathway for the decarboxylation of succinate to propionate. The Clostridium kluyveri CAT1 protein has been characterized as a acetyl-CoA:succinate CoA transferase and is believed to be involved in anaerobic succinate degradation. The propionate:succinate transferase activity has been reported in the propionic acid fermentation of propionibacterium species, where it is distinct from the coupled activities of distinct nucleotide-triphosphate dependent succinate and propionate/acetate CoA transferases (as inferred from activity in the absence of NTPs). The family represented by this model includes a member from Propionibacterium acnes KPA171202 which is likely to be responsible for this activity. A closely related clade not included in this family are the Ach1p proteins of fungi which are acetyl-CoA hydrolases. This name has been applied to many of the proteins represented by this model, possibly erroneously.
:
Pssm-ID: 274588 [Multi-domain] Cd Length: 485 Bit Score: 854.63 E-value: 0e+00
succinate CoA transferase; This family of CoA transferases includes enzymes catalyzing at ...
14-493
0e+00
succinate CoA transferase; This family of CoA transferases includes enzymes catalyzing at least two related but distinct activities. The E. coli YgfH protein has been characterized as a propionyl-CoA:succinate CoA transferase where it appears to be involved in a pathway for the decarboxylation of succinate to propionate. The Clostridium kluyveri CAT1 protein has been characterized as a acetyl-CoA:succinate CoA transferase and is believed to be involved in anaerobic succinate degradation. The propionate:succinate transferase activity has been reported in the propionic acid fermentation of propionibacterium species, where it is distinct from the coupled activities of distinct nucleotide-triphosphate dependent succinate and propionate/acetate CoA transferases (as inferred from activity in the absence of NTPs). The family represented by this model includes a member from Propionibacterium acnes KPA171202 which is likely to be responsible for this activity. A closely related clade not included in this family are the Ach1p proteins of fungi which are acetyl-CoA hydrolases. This name has been applied to many of the proteins represented by this model, possibly erroneously.
Pssm-ID: 274588 [Multi-domain] Cd Length: 485 Bit Score: 854.63 E-value: 0e+00
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which ...
329-464
7.87e-54
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.
Pssm-ID: 433126 [Multi-domain] Cd Length: 154 Bit Score: 178.02 E-value: 7.87e-54
succinate CoA transferase; This family of CoA transferases includes enzymes catalyzing at ...
14-493
0e+00
succinate CoA transferase; This family of CoA transferases includes enzymes catalyzing at least two related but distinct activities. The E. coli YgfH protein has been characterized as a propionyl-CoA:succinate CoA transferase where it appears to be involved in a pathway for the decarboxylation of succinate to propionate. The Clostridium kluyveri CAT1 protein has been characterized as a acetyl-CoA:succinate CoA transferase and is believed to be involved in anaerobic succinate degradation. The propionate:succinate transferase activity has been reported in the propionic acid fermentation of propionibacterium species, where it is distinct from the coupled activities of distinct nucleotide-triphosphate dependent succinate and propionate/acetate CoA transferases (as inferred from activity in the absence of NTPs). The family represented by this model includes a member from Propionibacterium acnes KPA171202 which is likely to be responsible for this activity. A closely related clade not included in this family are the Ach1p proteins of fungi which are acetyl-CoA hydrolases. This name has been applied to many of the proteins represented by this model, possibly erroneously.
Pssm-ID: 274588 [Multi-domain] Cd Length: 485 Bit Score: 854.63 E-value: 0e+00
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which ...
329-464
7.87e-54
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.
Pssm-ID: 433126 [Multi-domain] Cd Length: 154 Bit Score: 178.02 E-value: 7.87e-54
Acetyl-CoA hydrolase/transferase N-terminal domain; This family contains several enzymes which ...
11-215
1.26e-32
Acetyl-CoA hydrolase/transferase N-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.
Pssm-ID: 251367 Cd Length: 198 Bit Score: 123.03 E-value: 1.26e-32
Citrate lyase, alpha subunit (CitF); In citrate-utilizing prokaryotes, citrate lyase EC:4.1.3.6 cleaves intracellular citrate into acetate and oxaloacetate, and is organized as a functional complex consisting of alpha, beta, and gamma subunits. The gamma subunit serves as an acyl carrier protein (ACP), and has a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group. The citrate lyase is active only if this prosthetic group is acetylated; this acetylation is catalyzed by an acetate:SH-citrate lyase ligase. The alpha subunit substitutes citryl for the acetyl group to form citryl-S-ACP. The beta subunit completes the reaction by cleaving the citryl to yield oxaloacetate and (regenerated) acetyl-S-ACP. This family represents the alpha subunit EC:2.8.3.10.
Pssm-ID: 427798 [Multi-domain] Cd Length: 466 Bit Score: 42.50 E-value: 4.69e-04
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.
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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,
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(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.
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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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