CAZyme Information: Afu3g07210-T-p1

Basic Information

• Species: Aspergillus fumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus
• CAZyme ID: Afu3g07210-T-p1
• CAZy Family: GH172
• CAZyme Description: Has domain(s) with predicted hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds activity and role in carbohydrate metabolic process

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
452	Chr3_A_fumigatus_Af293|CGC15	51553.21	6.6153

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfumigatusAf293	10130	330879	290	9840

• Gene Location: location=Chr3_A_fumigatus_Af293:1812016-1813475(+)

Full Sequence      

MDLQGHLKWTGLISILSLMSLVNASPSITSTQNTNISACQQHAGLQSNDNTRNTRKVSLL
NGLHHQPPLVIDTFNDAWRNNLGFWHGAGEGLPFEYGNGYVRFFPTDPDHNYHTQLAAAE
CFSLLPYSDQYLHVVFSGTNKFSISLNQNNEDCDPYRKPYPETWDSVEASRYTSGNEIYV
PLSHFHIDQSRVLSISFNGFYSKESLTLYKVEIVPELPMGLRVPNRLANGRMVLRCTRPN
SFAFGIDDGQPCFAQEVMAILQKENILVTFFVVGSGLRDEETNFTQVYREMLRRGHQIAL
HSNTHRKMEGLEAIEDIDDEIIRNIRAFGSFLGVESRYFRPPFGTIGSRTRQRLAVYTSD
PQIVNWSVDIEDWLWGDTETPERQLEAFYRDVRRGGNLAVMHYLKPSTVKYFPQVIRFVK
AMNLTIMRIDQCLEDPSSPPLRVGRLNAISSP

Enzyme Prediction     

No EC number prediction in Afu3g07210-T-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	238	352	1e-19	0.8307692307692308

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
213022	CE4_NodB_like_6s_7s	6.60e-37	240	420	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	1.73e-29	236	424	4	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.
200576	CE4_MrCDA_like	3.41e-23	240	416	1	174	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.
200569	CE4_SmPgdA_like	4.37e-23	246	421	7	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	1.59e-22	243	416	4	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANH22692.1|CE4	1.76e-20	205	436	3	239
QBZ59347.1|CBM18|CE4	1.64e-19	230	437	62	268
BAI44125.1|CBM18|CE4	1.64e-19	230	437	62	268
SDR77466.1|CE4	5.98e-19	240	434	67	251
AII40413.1|CE4	1.35e-18	243	445	90	279

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7FBW_A	1.84e-15	243	434	120	301	Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
7AX7_A	7.79e-12	243	440	7	193	Crystal structure of the Xyl-CE4 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides [uncultured bacterium]
2IW0_A	9.80e-09	230	435	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|P83513|XY11A_PSEXY	2.46e-10	243	434	405	585	Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A PE=1 SV=2
sp|J9VPD7|CDA1_CRYNH	2.64e-10	233	388	152	311	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|P50325|CDA_AMYRO	2.26e-09	233	425	150	353	Chitin deacetylase OS=Amylomyces rouxii OX=29923 GN=CDA PE=1 SV=1
sp|Q6DWK3|CDA_COLLN	4.74e-08	230	435	32	240	Chitin deacetylase OS=Colletotrichum lindemuthianum OX=290576 GN=CDA PE=1 SV=1
sp|Q06702|CDA1_YEAST	1.32e-07	247	373	115	231	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
0.000221	0.999759	CS pos: 24-25. Pr: 0.9786

TMHMM  Annotations     

There is no transmembrane helices in Afu3g07210-T-p1.