GD15482 [Drosophila simulans]
Protein Classification
polysaccharide deacetylase family protein( domain architecture ID 79029)
metal-dependent polysaccharide deacetylase family protein, belonging to the carbohydrate esterase 4 (CE4) superfamily, may catalyze the N- or O-deacetylation of a substrate such as acetylated chitin, peptidoglycan, and acetylated xylan
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| CE4_SF super family | cl15692 | Catalytic NodB homology domain of the carbohydrate esterase 4 superfamily; The carbohydrate ... |
18-238 | 5.11e-131 | ||||
Catalytic NodB homology domain of the carbohydrate esterase 4 superfamily; The carbohydrate esterase 4 (CE4) superfamily mainly includes chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan, respectively. Members in this superfamily contain a NodB homology domain that adopts a deformed (beta/alpha)8 barrel fold, which encompasses a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad, closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The NodB homology domain of CE4 superfamily is remotely related to the 7-stranded beta/alpha barrel catalytic domain of the superfamily consisting of family 38 glycoside hydrolases (GH38), family 57 heat stable retaining glycoside hydrolases (GH57), lactam utilization protein LamB/YcsF family proteins, and YdjC-family proteins. The actual alignment was detected with superfamily member cd10974: Pssm-ID: 472828 Cd Length: 269 Bit Score: 373.98 E-value: 5.11e-131
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| Name | Accession | Description | Interval | E-value | ||||
| CE4_CDA_like_1 | cd10974 | Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ... |
18-238 | 5.11e-131 | ||||
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding peritrophin-A domain (ChBD) and/or a low-density lipoprotein receptor class A domain (LDLa); Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. CDAs have been isolated and characterized from various bacterial and fungal species and belong to the larger carbohydrate esterase 4 (CE4) superfamily. This family includes many CDA-like proteins mainly from insects, which contain a putative CDA-like catalytic domain similar to the catalytic NodB homology domain of CE4 esterases. In addition to the CDA-like domain, family members contain two additional domains, a chitin-binding peritrophin-A domain (ChBD) and a low-density lipoprotein receptor class A domain (LDLa), or have the ChBD domain but do not have the LDLa domain. Pssm-ID: 200596 Cd Length: 269 Bit Score: 373.98 E-value: 5.11e-131
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| Name | Accession | Description | Interval | E-value | ||||
| CE4_CDA_like_1 | cd10974 | Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding ... |
18-238 | 5.11e-131 | ||||
Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding peritrophin-A domain (ChBD) and/or a low-density lipoprotein receptor class A domain (LDLa); Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. CDAs have been isolated and characterized from various bacterial and fungal species and belong to the larger carbohydrate esterase 4 (CE4) superfamily. This family includes many CDA-like proteins mainly from insects, which contain a putative CDA-like catalytic domain similar to the catalytic NodB homology domain of CE4 esterases. In addition to the CDA-like domain, family members contain two additional domains, a chitin-binding peritrophin-A domain (ChBD) and a low-density lipoprotein receptor class A domain (LDLa), or have the ChBD domain but do not have the LDLa domain. Pssm-ID: 200596 Cd Length: 269 Bit Score: 373.98 E-value: 5.11e-131
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| CE4_CDA_like_2 | cd10975 | Putative catalytic domain of chitin deacetylase-like proteins; Chitin deacetylases (CDAs, EC 3. ... |
5-238 | 3.47e-69 | ||||
Putative catalytic domain of chitin deacetylase-like proteins; Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. CDAs have been isolated and characterized from various bacterial and fungal species and belong to the larger carbohydrate esterase 4 (CE4) superfamily. This family includes many midgut-specific CDA-like proteins mainly from insects, such as Tribolium castaneum CDAs (TcCDA6-9). These proteins contain a putative CDA-like catalytic domain similar to the catalytic NodB homology domain of CE4 esterases. In addition to the CDA-like domain, some family members have an additional chitin-binding peritrophin-A domain (ChBD). Pssm-ID: 200597 Cd Length: 268 Bit Score: 216.80 E-value: 3.47e-69
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| CE4_CDA_like | cd10919 | Putative catalytic domain of chitin deacetylase-like proteins from insects and similar ... |
17-238 | 5.84e-56 | ||||
Putative catalytic domain of chitin deacetylase-like proteins from insects and similar proteins; Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. CDAs have been isolated and characterized from various bacterial and fungal species and belong to the larger carbohydrate esterase family 4 (CE4). This family includes many CDA-like proteins, mainly from insects, which contain a putative CDA-like catalytic domain similar to the catalytic NodB homology domain of CE4 esterases. Some family members have an additional chitin binding domain (ChBD), or an additional low-density lipoprotein receptor class A domain (LDLa), or both. Due to the lack of some catalytically relevant residues, several insect CDA-like proteins are devoid of enzymatic activity and may simply bind to chitin and thus influence the mechanical or permeability properties of chitin-containing structures such as the cuticle or the peritrophic membrane. This family also includes many uncharacterized hypothetical proteins from bacteria, exhibiting high sequence similarity to insect CDA-like proteins. Pssm-ID: 200545 [Multi-domain] Cd Length: 273 Bit Score: 182.95 E-value: 5.84e-56
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| CE4_PuuE_HpPgdA_like_2 | cd10941 | Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar ... |
30-197 | 3.72e-07 | ||||
Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar to bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA); This family contains many uncharacterized prokaryotic polysaccharide deacetylases (DCAs) that show high sequence similarity to the catalytic domain of bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as homotetramers. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCA-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, PuuE allantoinase and HpPgdA do not exhibit a solvent-accessible polysaccharide binding groove and might only bind a small molecule at the active site. Pssm-ID: 200566 [Multi-domain] Cd Length: 258 Bit Score: 50.37 E-value: 3.72e-07
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| CE4_CDA_like_3 | cd10976 | Putative catalytic domain of uncharacterized bacterial hypothetical proteins similar to insect ... |
30-197 | 4.30e-05 | ||||
Putative catalytic domain of uncharacterized bacterial hypothetical proteins similar to insect chitin deacetylase-like proteins; The family includes many uncharacterized bacterial hypothetical proteins that show high sequence similarity to insect chitin deacetylase-like proteins. Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. Pssm-ID: 200598 [Multi-domain] Cd Length: 299 Bit Score: 44.66 E-value: 4.30e-05
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