cl00281: metallo-dependent_hydrolases Superfamily 
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Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Taxonomy: root
PubMed: 77 links
Protein: Related Protein
Related Structure
Accession: cl00281
PSSM Id: 260323
Name: metallo-dependent_hydrolases
Created: 8-Feb-2008
Updated: 16-Jan-2014
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Curated CD Hierarchy
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CD Hierarchy
Imported CD
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Citing CDD
Marchler-Bauer A et al. (2013), "CDD: conserved domains and protein three-dimensional structure.", Nucleic Acids Res. 41(D1):D384-52.
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