|PROSITE documentation PDOC51677 [for PROSITE entry PS51677]|
The NodB homology domain is a catalytic domain of ~200 amino acid residues, which has been named after its similarity to rhizobial NodB chitooligosaccharide deacetylase. It is found in members of carbohydrate esterase family 4 (CE4) [E1] and in PuuE proteins.
Members of the CE4 family exhibit metal-dependent deacetylation of O- and N-acetylated polysaccharides, such as chitin, peptidoglycan, and acetylxylan. Proteins belonging to this family have conserved residues that are important for metal coordination (D-H-H triad) and enzymatic activity. CE4 enzymes typically require a divalent Zn(2+) or Ni(2+) metal ion that is usually coordinated by an aspartate and two histidine residues [1,2,3,4].
PuuE proteins are allantoinases that catalyze the hydrolytic cleavage of the hydantoin ring of allantoin. The conserved D-H-H metal-binding triad is replaced by E-H-W in PuuE proteins. Amino acid substitutions are also observed for residues that have been implicated in catalysis, conferring metal independency to the enzyme .
The NodB homology domain adopts a deformed (β/α) barrel fold comprising eight parallel β-strands, with the C-terminal ends of five of these strands forming the solvent-exposed active site region, surrounded by eight α-helices (see <PDB:2W3Z>) [2,3,4].
The profile we developed covers the entire NodB homology domain.Last update:
June 2013 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Caufrier F. Martinou A. Dupont C. Bouriotis V.|
|Title||Carbohydrate esterase family 4 enzymes: substrate specificity.|
|Source||Carbohydr. Res. 338:687-692(2003).|
|2||Authors||Blair D.E. van Aalten D.M.F.|
|Title||Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N-acetyl-glucosamine.|
|Source||FEBS Lett. 570:13-19(2004).|
|3||Authors||Deng D.M. Urch J.E. ten Cate J.M. Rao V.A. van Aalten D.M. Crielaard W.|
|Title||Streptococcus mutans SMU.623c codes for a functional, metal-dependent polysaccharide deacetylase that modulates interactions with salivary agglutinin.|
|Source||J. Bacteriol. 191:394-402(2009).|
|4||Authors||Shaik M.M. Cendron L. Percudani R. Zanotti G.|
|Title||The structure of Helicobacter pylori HP0310 reveals an atypical peptidoglycan deacetylase.|
|Source||PLoS ONE 6:E19207-E19207(2011).|
|5||Authors||Ramazzina I. Cendron L. Folli C. Berni R. Monteverdi D. Zanotti G. Percudani R.|
|Title||Logical identification of an allantoinase analog (puuE) recruited from polysaccharide deacetylases.|
|Source||J. Biol. Chem. 283:23295-23304(2008).|