Summary: Linear amide C-N hydrolases, choloylglycine hydrolase family
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This is the Wikipedia entry entitled "Choloylglycine hydrolase family". More...
Choloylglycine hydrolase family Edit Wikipedia article
CBAH | |||||||||
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![]() penicillin v acylase from b. sphaericus | |||||||||
Identifiers | |||||||||
Symbol | CBAH | ||||||||
Pfam | PF02275 | ||||||||
Pfam clan | CL0052 | ||||||||
InterPro | IPR003199 | ||||||||
MEROPS | C89 | ||||||||
SCOPe | 3pva / SUPFAM | ||||||||
CDD | cd01935 | ||||||||
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In molecular biology, the choloylglycine hydrolase family is a family of linear amide C-N hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. It includes conjugated bile acid hydrolase (CBAH) EC 3.5.1.24, N-acylethanolamine acid amide hydrolase (NAAA) EC 3.5.1.- and penicillin acylase EC 3.5.1.11.[1][2]
References
- ^ Coleman JP, Hudson LL (1995). "Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens". Appl Environ Microbiol. 61 (7): 2514–20. PMC 167523. PMID 7618863.
- ^ Rossocha M, Schultz-Heienbrok R, von Moeller H, Coleman JP, Saenger W (2005). "Conjugated bile acid hydrolase is a tetrameric N-terminal thiol hydrolase with specific recognition of its cholyl but not of its tauryl product". Biochemistry. 44 (15): 5739–48. doi:10.1021/bi0473206. PMID 15823032.
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Linear amide C-N hydrolases, choloylglycine hydrolase family Provide feedback
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, PF15508.
Literature references
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Coleman JP, Hudson LL; , Appl Environ Microbiol 1995;61:2514-2520.: Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens. PUBMED:7618863 EPMC:7618863
Internal database links
SCOOP: | AAT |
Similarity to PfamA using HHSearch: | AAT |
External database links
MEROPS: | C89 |
SCOP: | 3pva |
This tab holds annotation information from the InterPro database.
InterPro entry IPR029132
This domain can be found in several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) ( EC ), penicillin acylase ( EC ) and acid ceramidase ( EC ). This domain is also found at the C terminus of acid ceramidase (AC) and N-acylethanolamine-hydrolysing acid amidase (NAAA) [ PUBMED:15655246 ]. AC and NAAA can be cleaved into two chains: alpha and beta. This domain represent the alpha subunit (chain).
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan NTN (CL0052), which has the following description:
In the N-terminal nucleophile aminohydrolases (Ntn hydrolases) the N-terminal residue provides two catalytic groups, nucleophile and proton donor. These enzymes use the side chain of the amino-terminal residue, incorporated in a beta-sheet, as the nucleophile in the catalytic attack at the carbonyl carbon. The nucleophile is cysteine in GAT, serine in penicillin acylase, and threonine in the proteasome. All the enzymes share an unusual fold in which the nucleophile and other catalytic groups occupy equivalent sites. This fold provides both the capacity for nucleophilic attack and the possibility of autocatalytic processing [1].
The clan contains the following 16 members:
AAT Asparaginase_2 CBAH DUF1933 DUF3700 G_glu_transpept GATase_2 GATase_4 GATase_6 GATase_7 IMP_cyclohyd Penicil_amidase Peptidase_C69 Phospholip_B Proteasome Proteasome_A_NAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (8) |
Full (3018) |
Representative proteomes | UniProt (13574) |
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RP15 (448) |
RP35 (1382) |
RP55 (2839) |
RP75 (4841) |
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HTML | |||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (8) |
Full (3018) |
Representative proteomes | UniProt (13574) |
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RP15 (448) |
RP35 (1382) |
RP55 (2839) |
RP75 (4841) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_5806 (release 5.2) |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Mian N |
Number in seed: | 8 |
Number in full: | 3018 |
Average length of the domain: | 259.60 aa |
Average identity of full alignment: | 21 % |
Average coverage of the sequence by the domain: | 74.96 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 316 | ||||||||||||
Family (HMM) version: | 20 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CBAH domain has been found. There are 117 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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