Species | Malassezia sympodialis | |||||||||||
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Lineage | Basidiomycota; Malasseziomycetes; ; Malasseziaceae; Malassezia; Malassezia sympodialis | |||||||||||
CAZyme ID | SHO77371.1 | |||||||||||
CAZy Family | GH128 | |||||||||||
CAZyme Description | Chitin deacetylase [Source:UniProtKB/TrEMBL;Acc:M5E9B1] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.5.1.41:2 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE4 | 161 | 278 | 1.9e-25 | 0.8923076923076924 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
200576 | CE4_MrCDA_like | 2.23e-87 | 162 | 345 | 1 | 178 | Catalytic NodB homology domain of Mucor rouxii chitin deacetylase and similar proteins. This family is represented by the chitin deacetylase (MrCDA, EC 3.5.1.41) encoded from the fungus Mucor rouxii (also known as Amylomyces rouxii). MrCDA is an acidic glycoprotein with a very stringent specificity for beta1-4-linked N-acetylglucosamine homopolymers. It requires at least four residues (chitotetraose) for catalysis, and can achieve extensive deacetylation on chitin polymers. MrCDA shows high sequence similarity to Colletotrichum lindemuthianum chitin deacetylase (endo-chitin de-N-acetylase, ClCDA), which consists of a single catalytic domain similar to the deformed (beta/alpha)8 barrel fold adopted by the carbohydrate esterase 4 (CE4) superfamily, 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 family also includes some uncharacterized eukaryotic and bacterial homologs of MrCDA. |
213022 | CE4_NodB_like_6s_7s | 5.35e-46 | 166 | 333 | 5 | 159 | Catalytic NodB homology domain of rhizobial NodB-like proteins. This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as 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. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ 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. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal. |
396211 | Polysacc_deac_1 | 3.57e-41 | 158 | 279 | 3 | 124 | Polysaccharide deacetylase. This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyzes glucosidic bonds in xylan. |
200575 | CE4_ClCDA_like | 6.14e-36 | 156 | 348 | 2 | 191 | Catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase and similar proteins. This family is represented by the chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41) from Colletotrichum lindemuthianum (also known as Glomerella lindemuthiana), which is a member of the carbohydrate esterase 4 (CE4) superfamily. ClCDA catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. It consists of a single catalytic domain similar to the deformed (alpha/beta)8 barrel fold adopted by other CE4 esterases, 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. It possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite affinity. Unlike its bacterial homologs, ClCDA contains two intramolecular disulfide bonds that may add stability to this secreted protein. The family also includes many uncharacterized deacetylases and hypothetical proteins mainly from eukaryotes, which show high sequence similarity to ClCDA. |
200584 | CE4_GT2-like | 8.70e-31 | 166 | 327 | 5 | 161 | Catalytic NodB homology domain of uncharacterized bacterial glycosyl transferase, group 2-like family proteins. This family includes many uncharacterized bacterial proteins containing an N-terminal GH18 (glycosyl hydrolase, family 18) domain, a middle NodB-like homology domain, and a C-terminal GT2-like (glycosyl transferase group 2) domain. Although their biological function is unknown, members in this family contain a middle NodB homology domain that is similar to the catalytic domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Like SpPgdA, this family is a member of the carbohydrate esterase 4 (CE4) superfamily. The presence of three domains suggests that members of this family may be multifunctional. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 475 | 1 | 475 | |
2.79e-242 | 4 | 428 | 6 | 433 | |
4.41e-161 | 60 | 416 | 8 | 362 | |
2.64e-140 | 42 | 392 | 33 | 387 | |
3.74e-140 | 42 | 392 | 33 | 387 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5.39e-22 | 166 | 346 | 121 | 288 | Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4] |
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9.00e-19 | 147 | 359 | 221 | 417 | Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) [Streptococcus pneumoniae R6] |
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9.54e-19 | 158 | 340 | 36 | 208 | Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88] |
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3.89e-18 | 147 | 359 | 221 | 417 | Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) D 275 N Mutant. [Streptococcus pneumoniae R6] |
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4.59e-18 | 165 | 334 | 8 | 162 | Family 4 carbohydrate esterase from Streptomyces lividans in complex with acetate [Streptomyces lividans],2CC0_B Family 4 carbohydrate esterase from Streptomyces lividans in complex with acetate [Streptomyces lividans] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.73e-102 | 12 | 380 | 12 | 374 | Chitin deacetylase 2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CDA2 PE=1 SV=1 |
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2.57e-99 | 12 | 380 | 13 | 375 | Chitin deacetylase 2 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=CDA2 PE=1 SV=1 |
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3.09e-87 | 54 | 367 | 28 | 359 | Chitin deacetylase OS=Amylomyces rouxii OX=29923 GN=CDA PE=1 SV=1 |
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3.09e-45 | 132 | 335 | 135 | 339 | Chitin deacetylase 1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CDA1 PE=1 SV=1 |
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8.05e-37 | 151 | 343 | 113 | 305 | Chitin deacetylase 3 OS=Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) OX=214684 GN=CDA3 PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.000328 | 0.999674 | CS pos: 19-20. Pr: 0.9739 |
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