{PDOC51677} {PS51677; NODB} {BEGIN} ******************************** * NodB homology domain profile * ******************************** 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 [5]. The NodB homology domain adopts a deformed (beta/alpha) barrel fold comprising eight parallel beta-strands, with the C-terminal ends of five of these strands forming the solvent-exposed active site region, surrounded by eight alpha- helices (see ) [2,3,4]. The profile we developed covers the entire NodB homology domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: June 2013 / First entry. [ 1] Caufrier F., Martinou A., Dupont C., Bouriotis V. "Carbohydrate esterase family 4 enzymes: substrate specificity." Carbohydr. Res. 338:687-692(2003). PubMed=12644381 [ 2] Blair D.E., van Aalten D.M.F. "Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N-acetyl-glucosamine." FEBS Lett. 570:13-19(2004). PubMed=15251431; DOI=10.1016/j.febslet.2004.06.013 [ 3] Deng D.M., Urch J.E., ten Cate J.M., Rao V.A., van Aalten D.M., Crielaard W. "Streptococcus mutans SMU.623c codes for a functional, metal-dependent polysaccharide deacetylase that modulates interactions with salivary agglutinin." J. Bacteriol. 191:394-402(2009). PubMed=18978064; DOI=10.1128/JB.00838-08 [ 4] Shaik M.M., Cendron L., Percudani R., Zanotti G. "The structure of Helicobacter pylori HP0310 reveals an atypical peptidoglycan deacetylase." PLoS ONE 6:E19207-E19207(2011). PubMed=21559431; DOI=10.1371/journal.pone.0019207 [ 5] Ramazzina I., Cendron L., Folli C., Berni R., Monteverdi D., Zanotti G., Percudani R. "Logical identification of an allantoinase analog (puuE) recruited from polysaccharide deacetylases." J. Biol. Chem. 283:23295-23304(2008). PubMed=18550550; DOI=10.1074/jbc.M801195200 [E1] http://www.cazy.org/CE4.html -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}