linear amide C-N hydrolase similar to choloylglycine hydrolase (CGH), a bile salt-modifying enzyme that hydrolyzes non-peptide carbon-nitrogen bonds in choloylglycine and choloyltaurine, both of which are present in bile
Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide ...
23-300
1.75e-160
Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide carbon-nitrogen bonds in choloylglycine and choloyltaurine, both of which are present in bile. CGH is present in a number of probiotic microbial organisms that inhabit the gut. CGH has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which CGH belongs.
:
Pssm-ID: 238885 Cd Length: 291 Bit Score: 449.09 E-value: 1.75e-160
Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide ...
23-300
1.75e-160
Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide carbon-nitrogen bonds in choloylglycine and choloyltaurine, both of which are present in bile. CGH is present in a number of probiotic microbial organisms that inhabit the gut. CGH has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which CGH belongs.
Pssm-ID: 238885 Cd Length: 291 Bit Score: 449.09 E-value: 1.75e-160
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
24-300
6.61e-39
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) EC:3.5.1.24, penicillin acylase EC:3.5.1.11 and acid ceramidase EC:3.5.1.23. This domain forms the alpha-subunit for members from vertebral species, see family NAAA-beta, pfam15508.
Pssm-ID: 396726 Cd Length: 316 Bit Score: 139.57 E-value: 6.61e-39
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
24-284
2.08e-12
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.
Pssm-ID: 468523 [Multi-domain] Cd Length: 312 Bit Score: 66.54 E-value: 2.08e-12
Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide ...
23-300
1.75e-160
Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide carbon-nitrogen bonds in choloylglycine and choloyltaurine, both of which are present in bile. CGH is present in a number of probiotic microbial organisms that inhabit the gut. CGH has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which CGH belongs.
Pssm-ID: 238885 Cd Length: 291 Bit Score: 449.09 E-value: 1.75e-160
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins ...
24-267
3.08e-63
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins includes conjugated bile acid hydrolase (CBAH), penicillin V acylase (PVA), acid ceramidase (AC), and N-acylethanolamine-hydrolyzing acid amidase (NAAA) which cleave non-peptide carbon-nitrogen bonds in bile salt constituents. These enzymes have an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which they belong. This nucleophilic cysteine is exposed by post-translational prossessing of the precursor protein.
Pssm-ID: 238910 Cd Length: 229 Bit Score: 199.89 E-value: 3.08e-63
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
24-294
4.55e-42
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), catalyzes the hydrolysis of penicillin V to yield 6-amino penicillanic acid (6-APA), an important key intermediate of semisynthetic penicillins. PVA has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which PVA belongs. This nucleophilic cysteine is exposed by post-translational prossessing of the PVA precursor. PVA forms a homotetramer.
Pssm-ID: 238303 Cd Length: 303 Bit Score: 147.36 E-value: 4.55e-42
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
24-300
6.61e-39
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) EC:3.5.1.24, penicillin acylase EC:3.5.1.11 and acid ceramidase EC:3.5.1.23. This domain forms the alpha-subunit for members from vertebral species, see family NAAA-beta, pfam15508.
Pssm-ID: 396726 Cd Length: 316 Bit Score: 139.57 E-value: 6.61e-39
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
24-284
2.08e-12
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.
Pssm-ID: 468523 [Multi-domain] Cd Length: 312 Bit Score: 66.54 E-value: 2.08e-12
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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