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PROSITE documentation PDOC50263 [for PROSITE entry PS50263] |
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 catalyze, these enzymes can be classified into functionally distinct groups including [1,2]:
The carbon-nitrogen hydrolase domain can be found alone or associated with other domains, such as the NAD synthase domain, the HIT histidine triad (see <PDOC00694>), the acetyltransferase domain or the glycosyltransferase domain.
The carbon-nitrogen hydrolase domain is characterized 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 [1].
The profile we developed covers the entire carbon-nitrogen hydrolase domain.
Last update:March 2017 / Profile revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Bork P. Koonin E.V. |
Title | A new family of carbon-nitrogen hydrolases. | |
Source | Protein Sci. 3:1344-1346(1994). | |
PubMed ID | 7987228 |
2 | Authors | Fujii T. Ahn J.-Y. Kuse M. Mori H. Matsuda T. Isobe M. |
Title | A novel photoprotein from oceanic squid (Symplectoteuthis oualaniensis) with sequence similarity to mammalian carbon-nitrogen hydrolase domains. | |
Source | Biochem. Biophys. Res. Commun. 293:874-879(2002). | |
PubMed ID | 12054553 | |
DOI | 10.1016/S0006-291X(02)00296-6 |