CAZyme Information: KAG2013658.1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: KAG2013658.1
• CAZy Family: GH18
• CAZyme Description: chitin deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
498		54263.12	4.7977

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ccinerea326	15250	N/A	238	15012

• Gene Location: location=JAAGWA010000005:1773744-1775469(+)

Full Sequence      

MLLSTLFAFLPLVSAVTVPALNDRHDSHEHVQPGALPERWYQDDSHPVHRLFKRATDDGI
AYPPVGSPEWSAPFPQGVPDPAFLPQDWVDALNAAVEAGRIPDIPLAVSERPQTNPVYPA
TVNPTSPEVCSTTYKCRGPEDLWDAPDGVFASSFDDGPYPSSGRLVEFLSANNVKTTHFM
IGVHILANPSEFVAAFEADNDIAVHTWSHPYMTTLSNLDILGQLGWTMQLIHHSTGGRVP
RYWRPPYGDSDNRVRAIAKEVMLLFWESVGVLANGSCRFSAWKLSSGIWSERAVPPFPLI
TMLTPVTAPTTGGCQRALSPLNRLLNVSRVGSLVRYHTANLVVRFHLERSILGPKSPGLM
ILQHEVTDASIDVFMNVFPLIAQQGWEFGSLASVVGDRRAYQNAESSSSDDVFFKDIIVD
PAALTPSDDTGDSDYPAPTSDGLSEPTEGLTPTSDLETEGLQPTPTPPSSSSSARSLSLP
SSRRAWILSCSLFVGLLL

Enzyme Prediction     

No EC number prediction in KAG2013658.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	146	261	1.5e-17	0.8692307692307693

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200576	CE4_MrCDA_like	1.46e-47	153	259	6	111	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.
396211	Polysacc_deac_1	4.00e-26	144	260	3	118	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.
213022	CE4_NodB_like_6s_7s	1.84e-25	148	260	1	113	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.
200578	CE4_CtAXE_like	1.93e-21	151	266	4	118	Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its bacterial homologs. This family is represented by Clostridium thermocellum acetylxylan esterase (CtAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. CtAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan, as a consequence of deacetylation. CtAXE is a monomeric protein containing a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases. However, due to differences in the topography of the substrate-binding groove, the chemistry of the active center, and metal ion coordination, CtAXE has different metal ion preference and lacks activity on N-acetyl substrates. It is significantly activated by Co2+. Moreover, CtAXE displays distinctly different ligand coordination to the metal ion, utilizing an aspartate, a histidine, and four water molecules, as opposed to the conserved His-His-Asp zinc-binding triad of other CE4 esterases.
200575	CE4_ClCDA_like	4.63e-21	148	260	8	123	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VWO95489.1|CE4	4.60e-106	4	409	7	360
QRV73052.1|CE4	2.56e-87	6	409	4	352
QRV87921.1|CE4	7.15e-87	6	409	4	352
QRW02099.1|CE4	4.39e-85	6	409	4	352
QRW21168.1|CE4	1.59e-80	35	482	19	397

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2CC0_A	9.30e-14	145	257	2	113	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]
6H8L_A	4.31e-13	140	259	2	121	Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],6H8L_B Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
6H8N_A	2.66e-12	140	259	2	121	Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis - mutant D285S [Bacillus subtilis subsp. subtilis str. 168],6H8N_B Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis - mutant D285S [Bacillus subtilis subsp. subtilis str. 168]
7BLY_A	8.90e-10	151	249	43	140	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
7AX7_A	2.05e-09	149	247	5	103	Crystal structure of the Xyl-CE4 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides [uncultured bacterium]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P0CP76|CDA3_CRYNJ	1.18e-55	31	410	16	334	Chitin deacetylase 3 OS=Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) OX=214684 GN=CDA3 PE=2 SV=1
sp|P82476|CDA3_CRYNH	1.24e-55	38	410	23	334	Chitin deacetylase 3 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CDA3 PE=1 SV=3
sp|P0CP77|CDA3_CRYNB	3.35e-54	38	410	23	334	Chitin deacetylase 3 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=CDA3 PE=3 SV=1
sp|J9VPD7|CDA1_CRYNH	3.08e-28	136	268	146	280	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
sp|Q06702|CDA1_YEAST	1.93e-22	68	267	42	225	Chitin deacetylase 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=CDA1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000671	0.999271	CS pos: 15-16. Pr: 0.9646

TMHMM  Annotations     

There is no transmembrane helices in KAG2013658.1.