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42  structures 1418  species 1  interaction 2070  sequences 9  architectures

Family: CBAH (PF02275)

Summary: Linear amide C-N hydrolases, choloylglycine hydrolase family

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Choloylglycine hydrolase family". More...

Choloylglycine hydrolase family Edit Wikipedia article

CBAH
PDB 3pva EBI.jpg
penicillin v acylase from b. sphaericus
Identifiers
Symbol CBAH
Pfam PF02275
Pfam clan CL0052
InterPro IPR003199
MEROPS C89
SCOP 3pva
SUPERFAMILY 3pva

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 and penicillin acylase EC 3.5.1.11.[1][2]

References[edit]

  1. ^ 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. 
  2. ^ 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. 

This article incorporates text from the public domain Pfam and InterPro IPR003199

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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

  1. 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

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003199

This family of choloylglycine hydrolases includes conjugated bile acid hydrolase (CBAH) EC and penicillin acylase EC which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

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 14 members:

AAT Asparaginase_2 CBAH DUF1933 DUF3700 G_glu_transpept GATase_2 GATase_4 GATase_6 GATase_7 Penicil_amidase Peptidase_C69 Phospholip_B Proteasome

Alignments

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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

View options

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
(2070)
Representative proteomes NCBI
(1606)
Meta
(83)
RP15
(137)
RP35
(230)
RP55
(310)
RP75
(386)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(8)
Full
(2070)
Representative proteomes NCBI
(1606)
Meta
(83)
RP15
(137)
RP35
(230)
RP55
(310)
RP75
(386)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

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
(2070)
Representative proteomes NCBI
(1606)
Meta
(83)
RP15
(137)
RP35
(230)
RP55
(310)
RP75
(386)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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 View help on the curation process

Seed source: Pfam-B_5806 (release 5.2)
Previous IDs: none
Type: Domain
Author: Mian N, Bateman A, Griffiths-Jones SR
Number in seed: 8
Number in full: 2070
Average length of the domain: 285.70 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 86.92 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.4 20.4
Trusted cut-off 20.5 20.4
Noise cut-off 20.3 20.3
Model length: 316
Family (HMM) version: 13
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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Interactions

There is 1 interaction for this family. More...

CBAH

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 42 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 seqence.

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