acyl-CoA thioesterase/bile acid-CoA:amino acid N-acyltransferase (BAAT) family protein may catalyze the hydrolysis of acyl-CoA or catalyze the amidation of bile acids with the amino acids taurine and glycine
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
21-138
4.81e-29
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.
:
Pssm-ID: 461422 Cd Length: 127 Bit Score: 110.02 E-value: 4.81e-29
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
203-412
9.56e-24
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.
The actual alignment was detected with superfamily member pfam08840:
Pssm-ID: 473884 [Multi-domain] Cd Length: 211 Bit Score: 98.12 E-value: 9.56e-24
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
21-138
4.81e-29
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.
Pssm-ID: 461422 Cd Length: 127 Bit Score: 110.02 E-value: 4.81e-29
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
203-412
9.56e-24
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).
Pssm-ID: 430252 [Multi-domain] Cd Length: 211 Bit Score: 98.12 E-value: 9.56e-24
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini ...
21-138
4.81e-29
Acyl-CoA thioester hydrolase/BAAT N-terminal region; This family consists of the amino termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT). This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism. For example, in peroxisomes, the hydrolase acts on bile-CoA esters.
Pssm-ID: 461422 Cd Length: 127 Bit Score: 110.02 E-value: 4.81e-29
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
203-412
9.56e-24
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).
Pssm-ID: 430252 [Multi-domain] Cd Length: 211 Bit Score: 98.12 E-value: 9.56e-24
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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