CAZyme Information: GAQ04719.1

Basic Information

• Species: Aspergillus lentulus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus
• CAZyme ID: GAQ04719.1
• CAZy Family: CE3
• CAZyme Description: chitooligosaccharide deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
411	BCLY01000004|CGC16	46770.85	5.1572

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AlentulusIFM54703	9916	N/A	259	9657

• Gene Location: location=BCLY01000004:2269141-2270586(-)

Full Sequence      

MAAMDLQGHLKLAGLISIVSLISLVIASPSITSTQDTNIPPCQQHAELQSNDNTRNTRKV
SLLNGLGHEPPLVIDTFNDTWRNNLGFWHGAGEGLPIEYGDGYVRFFPTDPDHNYHTQLA
AAECFSFLPYSDQYLHIVFSGTNKFSISLNQNNEDCDPYRKPYPETWDSVEAARVLSVSF
NGFYSKESLTLYKVEIVPELPMGLRVPNRLANDDGQPRFAQEVMDILEKENILVTFFVVG
AGLRDEETNFTQVYREMLRRGHQIALHSNTHRKMEGLQAIEDIDDEIIRNIRAFGSFLGV
ESARYFRPPFGTIGSRTRQRLAVYTSDPQIVNWSVDIEDWLWGDTETPERQLEAFYRDVR
RGGNLAVMHYLKPSTVKYFPQVIRFVKAMNLTIMRIDQCLEDPSSPPLMVG

Enzyme Prediction     

No EC number prediction in GAQ04719.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	213	319	1.1e-18	0.7615384615384615

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
213022	CE4_NodB_like_6s_7s	5.38e-35	213	387	8	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	3.59e-26	206	391	6	192	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	2.12e-23	213	388	8	182	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	2.35e-22	213	383	8	164	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	2.28e-21	182	402	37	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
QBZ59347.1|CBM18|CE4	1.77e-18	210	404	76	268
BAI44125.1|CBM18|CE4	1.77e-18	210	404	76	268
AVR47489.1|CE4	8.42e-18	210	401	30	210
AII40413.1|CE4	1.16e-17	210	404	91	271
AYM72662.1|CE4	1.16e-17	210	404	91	271

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7FBW_A	1.19e-14	210	401	121	301	Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
7BLY_A	3.15e-14	207	405	39	232	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
7AX7_A	4.94e-12	210	407	8	193	Crystal structure of the Xyl-CE4 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides [uncultured bacterium]
2C1I_A	2.82e-11	212	400	243	416	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) D 275 N Mutant. [Streptococcus pneumoniae R6]
2C1G_A	4.99e-11	210	400	240	416	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P50355|NODB_SINFN	4.90e-11	210	340	22	146	Chitooligosaccharide deacetylase OS=Sinorhizobium fredii (strain NBRC 101917 / NGR234) OX=394 GN=nodB PE=3 SV=2
sp|P83513|XY11A_PSEXY	1.46e-10	210	401	406	585	Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A PE=1 SV=2
sp|A0A1L3THR9|CDA_PESTX	1.76e-10	206	405	37	233	Chitin deacetylase OS=Pestalotiopsis sp. OX=36460 GN=CDA PE=1 SV=1
sp|Q8DP63|PGDA_STRR6	2.78e-10	210	400	272	448	Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1
sp|P50352|NODB_BRAEL	6.54e-09	210	340	25	149	Chitooligosaccharide deacetylase OS=Bradyrhizobium elkanii OX=29448 GN=nodB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000696	0.999277	CS pos: 27-28. Pr: 0.9685

TMHMM  Annotations     

There is no transmembrane helices in GAQ04719.1.