CAZyme Information: ACLA_035150-t26_1-p1

Basic Information

• Species: Aspergillus clavatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus clavatus
• CAZyme ID: ACLA_035150-t26_1-p1
• CAZy Family: GH131
• CAZyme Description: polysaccharide deacetylase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
449		51025.89	6.4099

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AclavatusNRRL1	9428	344612	287	9141

• Gene Location: location=DS027056:562127-563582(+)

Full Sequence      

MAAIVAVYRLRWTRLVGILSFLCLVVAFPSNRTTQNGTYIPILPFHQHSTPPSAGTTPNC
TNISIPNGMDFHPTVMIDTFHDTYRNNLGFWHGPGEDLPVKYGGSYVRFFPSDPDHNYHT
QLASEGCFSLLPYQDQYLHVEFSGTNKFSISLNQNNRECDARRKPYPETWDSVEAARYAL
GHHIFVPLAHFHIDLSNVLSVSFNGFYTGETLTLHKVEIVSELPMRLRLPDKLESGSMVL
RCTRPNSFAFGIDDGLPQFAQQVMDILEKEGILVTFFVVGAGLRSEDTNFTQVYREMLRR
GHQIALHSDTHRKMEGLETIEDIDNEIIKNIQTFQGLLGVESRYFRPPFGTVGARLRQRL
AAHITDPQIVNWSVDIEDWLWAGTETPEKQLEAFYRDVRQGGNLAVMHYLSPSTVQYFPE
VIRFVKARNATIMRIDQCLEDPASPPLTG

Enzyme Prediction     

No EC number prediction in ACLA_035150-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	244	361	1.1e-20	0.8538461538461538

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
213022	CE4_NodB_like_6s_7s	4.07e-41	246	426	1	171	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	8.91e-35	242	429	4	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.
200569	CE4_SmPgdA_like	1.11e-25	252	428	7	183	Catalytic NodB homology domain of Streptococcus mutans polysaccharide deacetylase PgdA, Bacillus subtilis YheN, and similar proteins. This family is represented by a putative polysaccharide deacetylase PgdA from the oral pathogen Streptococcus mutans (SmPgdA) and Bacillus subtilis YheN (BsYheN), which are members of the carbohydrate esterase 4 (CE4) superfamily. SmPgdA is an extracellular metal-dependent polysaccharide deacetylase with a typical CE4 fold, with metal bound to a His-His-Asp triad. It possesses de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. SmPgdA plays a role in tuning cell surface properties and in interactions with (salivary) agglutinin, an essential component of the innate immune system, most likely through deacetylation of an as-yet-unidentified polysaccharide. SmPgdA shows significant homology to the catalytic domains of peptidoglycan deacetylases from Streptococcus pneumoniae (SpPgdA) and Listeria monocytogenes (LmPgdA), both of which are involved in the bacterial defense mechanism against human mucosal lysozyme. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. The biological function of BsYheN is still unknown. This family also includes many uncharacterized polysaccharide deacetylases mainly found in bacteria.
200578	CE4_CtAXE_like	3.88e-25	249	428	4	170	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.
223798	CDA1	5.46e-24	253	441	72	259	Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UDM82332.1|CE4	2.02e-21	249	445	91	274
UDM70644.1|CE4	2.02e-21	249	445	91	274
UDM78063.1|CE4	2.02e-21	249	445	91	274
UDM78949.1|CE4	4.04e-21	249	445	91	274
UDM73902.1|CE4	1.61e-20	249	445	85	268

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7BLY_A	8.30e-19	236	442	30	230	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
7FBW_A	3.64e-17	249	440	120	301	Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
2Y8U_A	8.34e-16	223	441	14	223	Chain A, CHITIN DEACETYLASE [Aspergillus nidulans],2Y8U_B Chain B, CHITIN DEACETYLASE [Aspergillus nidulans]
7AX7_A	3.22e-14	249	446	7	193	Crystal structure of the Xyl-CE4 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides [uncultured bacterium]
2IW0_A	9.08e-10	236	441	32	240	Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [Colletotrichum lindemuthianum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1L3THR9|CDA_PESTX	4.29e-16	236	444	29	233	Chitin deacetylase OS=Pestalotiopsis sp. OX=36460 GN=CDA PE=1 SV=1
sp|Q5AQQ0|CDA_EMENI	2.63e-15	219	441	17	230	Chitin deacetylase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=cda PE=1 SV=1
sp|P83513|XY11A_PSEXY	1.91e-11	249	440	405	585	Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A PE=1 SV=2
sp|A0A0H3GDH9|PGDA_LISM4	2.66e-11	223	437	250	444	Peptidoglycan-N-acetylglucosamine deacetylase PgdA OS=Listeria monocytogenes serotype 1/2a (strain 10403S) OX=393133 GN=pgdA PE=2 SV=1
sp|Q8Y9V5|PGDA_LISMO	2.66e-11	223	437	250	444	Peptidoglycan-N-acetylglucosamine deacetylase PgdA OS=Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) OX=169963 GN=pgdA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000883	0.999086	CS pos: 27-28. Pr: 0.9737

TMHMM  Annotations     

Start	End
12	29