CAZyme Information: ASPGLDRAFT_41904-t33_1-p1

Basic Information

• Species: Aspergillus glaucus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus glaucus
• CAZyme ID: ASPGLDRAFT_41904-t33_1-p1
• CAZy Family: GH47
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
470	KV878889|CGC5	50952.66	7.9431

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AglaucusCBS516.65	11429	1160497	175	11254

• Gene Location: location=KV878889:359910-361322(-)

Full Sequence      

MVAKAASCGARTSRIGVVPSTASAERASVARLPVSPSTASLRMRTTRRTDISLTGYCGSS
KAHCRSPDCQIDFGHCDALSSPEGPSTEKIRRPKIGTAPYGPNVIRSCAVPGTIALTFDD
GPREYTEELLGLLERYNAKATFFITGNNGGKGPIDDFDMPWSTLIKRMQLEGHQIASHTW
SHQDLSKISHDQRKDQLLKNEMALRNILGGFPTYMRPPYSSCLPESGCLDDLGKLGYHVV
LYDLDTSDYAHDSPDAIQVSKDIFNKAVDPWKVTDKSWLVIAHDVHEQTVHNLTEHMLRK
IRDRGYHAVTVGQCLNDPEEYWYRKDPHGPLHADKEGKESRKKDNKGKPSTFKAITLDGT
CGVNVTCVGSAFGPCCSSAGYCGNSTAHCGTGCQSDFGRCFWPDSDKLLPNGTTIGIPAK
PKDTAAGWLPIDKDKDAAKRPVKSEAGSLVKTGASVTALALLTSAVVLLG

Enzyme Prediction     

No EC number prediction in ASPGLDRAFT_41904-t33_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	112	240	9.3e-30	0.8923076923076924

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200575	CE4_ClCDA_like	1.48e-96	105	311	1	197	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.
213022	CE4_NodB_like_6s_7s	1.04e-45	112	293	1	163	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	1.49e-39	114	311	3	177	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	2.51e-39	114	326	67	267	Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
396211	Polysacc_deac_1	3.34e-38	111	240	6	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCR90332.1|CBM18|CE4	2.49e-294	52	469	70	487
QRD85364.1|CBM18|CE4	8.48e-164	52	470	69	454
QMW29082.1|CBM18|CE4	1.71e-162	56	470	69	450
QMW41157.1|CBM18|CE4	1.71e-162	56	470	69	450
BAE58811.1|CBM18|CE4	2.33e-162	52	464	69	448

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2IW0_A	1.96e-56	99	324	30	247	Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [Colletotrichum lindemuthianum]
7BLY_A	1.19e-52	99	324	28	236	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
2Y8U_A	1.82e-46	93	323	15	229	Chain A, CHITIN DEACETYLASE [Aspergillus nidulans],2Y8U_B Chain B, CHITIN DEACETYLASE [Aspergillus nidulans]
5LFZ_A	4.70e-29	108	315	21	204	T48 deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
2C1G_A	9.49e-25	114	326	238	430	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|A0A1L3THR9|CDA_PESTX	8.73e-57	84	400	12	297	Chitin deacetylase OS=Pestalotiopsis sp. OX=36460 GN=CDA PE=1 SV=1
sp|Q6DWK3|CDA_COLLN	1.66e-55	99	324	30	247	Chitin deacetylase OS=Colletotrichum lindemuthianum OX=290576 GN=CDA PE=1 SV=1
sp|D4B5F9|PGDA_ARTBC	5.38e-48	99	327	137	352	Probable peptidoglycan-N-acetylglucosamine deacetylase ARB_03699 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03699 PE=1 SV=2
sp|D4AM78|CDA_ARTBC	1.75e-47	93	324	150	368	Chitin deacetylase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=CDA PE=3 SV=1
sp|Q5AQQ0|CDA_EMENI	1.14e-45	93	323	22	236	Chitin deacetylase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=cda PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000055	0.000001

TMHMM  Annotations     

There is no transmembrane helices in ASPGLDRAFT_41904-t33_1-p1.