The domain within your query sequence starts at position 51 and ends at position 296; the E-value for the CN_hydrolase domain shown below is 6.9e-19.



PFAM accession number:PF00795
Interpro abstract (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 ), which cleave various nitriles into the corresponding acids and ammonia.
  • Cyanide hydratase ( EC ) of pathogenic fungi, which detoxifies HCN that is released by their hosts, cyanogenic plants, after injury.
  • Aliphatic amidases ( EC ), which enable prokaryotes to use acetamides as both carbon and nitrogen source.
  • Beta-ureidopropionase (also known as beta-alanine synthase or N-carbamoyl-beta-alanine amino hydrolase; EC ), which catalyses the last step of pyrimidine catabolism.
  • Glutamine-dependent NAD(+) synthetase (also known as AdgA, for ammonia-dependent growth) from Rhodobacter species ( EC ). It appears to be essential for using various amino acids as nitrogen sources.
  • Biotinidase ( EC ), which catalyses the hydrolysis of biocytin to biotin and lysine.
  • Pantetheinase ( EC ) (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 ([intenz:2.3.1.-]) (gene lnt), a bacterial enzyme that transfers the fatty acyl group on membrane lipoproteins.
  • Glutamine-dependent NAD(+) synthetase ( EC ), which catalyses the final step in NAD+ synthesis [ (PUBMED:12771147) (PUBMED:12898714) ].

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) ].

GO process:nitrogen compound metabolic process (GO:0006807)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry CN_hydrolase