succinate CoA transferase; This family of CoA transferases includes enzymes catalyzing at ...
5-490
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.
The actual alignment was detected with superfamily member TIGR03458:
Pssm-ID: 274588 [Multi-domain] Cd Length: 485 Bit Score: 747.16 E-value: 0e+00
succinate CoA transferase; This family of CoA transferases includes enzymes catalyzing at ...
5-490
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: 747.16 E-value: 0e+00
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which ...
321-462
3.72e-57
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: 186.88 E-value: 3.72e-57
succinate CoA transferase; This family of CoA transferases includes enzymes catalyzing at ...
5-490
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: 747.16 E-value: 0e+00
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which ...
321-462
3.72e-57
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: 186.88 E-value: 3.72e-57
Acetyl-CoA hydrolase/transferase N-terminal domain; This family contains several enzymes which ...
5-214
8.81e-25
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: 101.46 E-value: 8.81e-25
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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