Summary: Carbon-nitrogen hydrolase
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Carbon-nitrogen hydrolase Provide feedback
This family contains hydrolases that break carbon-nitrogen bonds [1]. The family includes: Nitrilase EC:3.5.5.1 Q42965 Aliphatic amidase EC:3.5.1.4 Q01360 Biotidinase EC:3.5.1.12 P43251 Beta-ureidopropionase EC:3.5.1.6 Q03248. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins [2].
Literature references
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Bork P, Koonin EV; , Protein Sci 1994;3:1344-1346.: A new family of carbon-nitrogen hydrolases. PUBMED:7987228 EPMC:7987228
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Pace HC, Brenner C; , Genome Biol 2001;2:REVIEWS0001.: The nitrilase superfamily: classification, structure and function. PUBMED:11380987 EPMC:11380987
External database links
| HOMSTRAD: | CN_hydrolase |
| PANDIT: | PF00795 |
| PROSITE: | PDOC00712 PDOC00943 |
| Pseudofam: | PF00795 |
| SCOP: | 1ems |
| SYSTERS: | CN_hydrolase |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003010
The carbon-nitrogen hydrolase domain is an around 265-residue domain found in numerous enzymes involved in the reduction of organic nitrogen compounds and ammonia production. Based on their sequence similarity and on the reactions they catalyse, these enzymes can be classified into functionally distinct groups including [PUBMED:7987228, PUBMED:12054553]:
- Nitrilases (EC 3.5.5.1), which cleave various nitriles into the corresponding acids and ammonia.
- Cyanide hydratase (EC 4.2.1.66) of pathogenic fungi, which detoxifies HCN that is released by their hosts, cyanogenic plants, after injury.
- Aliphatic amidases (EC 3.5.1.4), which enable prokaryotes to use acetamides as both carbon and nitrogen source.
- Beta-alanine synthase (N-carbamoyl-beta-alanine amino hydrolase) (EC 3.5.1.6), which catalyses the last step of pyrimidine catabolism.
- AdgA (for ammonia-dependent growth) from Rhodobacter species (EC 6.3.5.1). It appears to be essential for using various amino acids as nitrogen sources.
- Biotinidase (EC 3.5.1.12), which catalyses the hydrolysis of biocytin to biotin and lysine.
- Pantetheinase (EC 3.5.1.92) (Pantetheine hydrolase) (Vanin), which hydrolyzes specifically one of the carboamide linkages in D-pantetheine, thus recycling pantothenic acid (vitamin B5) and releasing cysteamine.
- Apolipoprotein N-acyltransferase (EC 2.3.1.-) (gene lnt), a bacterial enzyme that transfers the fatty acyl group on membrane lipoproteins.
The carbon-nitrogen hydrolase domain is characterised by several conserved motifs, one of which contains a cysteines that is part of the catalytic site in nitrilases. Another highly conserved motif includes a glutamic acid that might also be involved in catalysis [PUBMED:7987228].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds (GO:0016810) |
| Biological process | nitrogen compound metabolic process (GO:0006807) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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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 (58) |
Full (15146) |
Representative proteomes | NCBI (12501) |
Meta (4878) |
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| RP15 (1561) |
RP35 (3031) |
RP55 (4091) |
RP75 (4901) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Format an alignment
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 (58) |
Full (15146) |
Representative proteomes | NCBI (12501) |
Meta (4878) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (1561) |
RP35 (3031) |
RP55 (4091) |
RP75 (4901) |
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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.
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
| Seed source: | Pfam-B_1042 (release 2.1) & Pfam-B_5155 (Release 7.5) |
| Previous IDs: | Nitrilase; |
| Type: | Family |
| Author: | Bateman A |
| Number in seed: | 58 |
| Number in full: | 15146 |
| Average length of the domain: | 178.50 aa |
| Average identity of full alignment: | 18 % |
| Average coverage of the sequence by the domain: | 46.69 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 186 | ||||||||||||
| Family (HMM) version: | 17 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
CN_hydrolaseStructures
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 CN_hydrolase domain has been found. There are 101 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence