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CAZyme Information: AYO42617.1

You are here: Home > Sequence: AYO42617.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Malassezia restricta
Lineage Basidiomycota; Malasseziomycetes; ; Malasseziaceae; Malassezia; Malassezia restricta
CAZyme ID AYO42617.1
CAZy Family GH5
CAZyme Description Chitin deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
486 53005.17 6.2899
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_MrestrictaCBS7877 4155 425264 59 4096
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.5.1.41:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE4 164 281 1.6e-24 0.8923076923076924

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
200576 CE4_MrCDA_like 4.29e-84 166 340 2 177
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 2.36e-43 169 331 5 161
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.
200575 CE4_ClCDA_like 1.35e-38 158 335 1 181
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.
396211 Polysacc_deac_1 5.30e-37 161 282 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.
223798 CDA1 5.34e-29 169 323 69 222
Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 486 1 486
0.0 1 486 1 486
2.76e-168 1 413 1 402
1.02e-157 5 409 4 401
2.05e-157 9 409 6 401

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.26e-22 158 336 33 208
Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
2.31e-22 169 330 121 276
Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
3.76e-21 168 341 8 173
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]
9.74e-19 158 347 35 232
Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [Colletotrichum lindemuthianum]
1.17e-18 146 345 24 222
Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide [Bacillus cereus ATCC 14579],5NC9_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide [Bacillus cereus ATCC 14579],5NC9_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide [Bacillus cereus ATCC 14579],5NC9_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2,6-diamino-N-hydroxyhexanamide [Bacillus cereus ATCC 14579],5NCD_A Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide [Bacillus cereus],5NCD_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide [Bacillus cereus],5NCD_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide [Bacillus cereus],5NCD_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide [Bacillus cereus],5NEK_A Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with acetazolamide [Bacillus cereus],5NEK_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with acetazolamide [Bacillus cereus],5NEK_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with acetazolamide [Bacillus cereus],5NEK_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with acetazolamide [Bacillus cereus],5NEL_A Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with ThiametG [Bacillus cereus],5NEL_B Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with ThiametG [Bacillus cereus],5NEL_C Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with ThiametG [Bacillus cereus],5NEL_D Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with ThiametG [Bacillus cereus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.16e-93 56 377 58 376
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
8.85e-87 131 377 125 377
Chitin deacetylase 2 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=CDA2 PE=1 SV=1
1.20e-86 121 375 115 368
Chitin deacetylase OS=Amylomyces rouxii OX=29923 GN=CDA PE=1 SV=1
1.81e-41 137 309 139 314
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
1.92e-37 157 333 116 299
Chitin deacetylase 3 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=CDA3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.002577 0.997393 CS pos: 19-20. Pr: 0.9349

TMHMM  Annotations      help

There is no transmembrane helices in AYO42617.1.