CAZyme Information: HCDG_04619-t38_1-p1

Basic Information

• Species: Histoplasma capsulatum
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum
• CAZyme ID: HCDG_04619-t38_1-p1
• CAZy Family: GH47
• CAZyme Description: chitin deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
334	GG692424|CGC2	37431.18	6.2147

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HcapsulatumH143	9796	544712	249	9547

• Gene Location: location=GG692424:718884-719982(-)

Full Sequence      

MAEYYPTLRSPCRRYMFHPQDLEGWTIRPLWPCKNAMLLNRNVVQRMGLVRTVTAAHHPA
PDCLIDYGSGCDALRTPDGESTLSAPRDPLGKIPYANQPIFNCKVPNTVALTYDDGPNIY
TSDLLDILDSFGAKATFFVTGINSNKGPIDDHNLPWRGLINRMLNKHQIASHTWAHQNLD
SLSPDQLRSQLVKNEMALRNIFGGFPTYMRPPYSSCSDQSGCVQELNGLGYHVAYFDVDT
DDYNNDSPYLIQASKDIFDYALASAKPYGGPLLVIAHDVHKQTVYNLTSHMLDGIYAAGY
RAVTLGECLGDDPENWYRWIPSKNSQDHSVVNVV

Enzyme Prediction     

No EC number prediction in HCDG_04619-t38_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	106	234	8.7e-28	0.9

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200575	CE4_ClCDA_like	2.88e-87	100	305	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	9.38e-43	107	284	1	160	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	2.75e-33	109	307	3	179	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.
396211	Polysacc_deac_1	1.24e-32	106	234	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.
200582	CE4_NodB_like_3	1.06e-30	109	305	3	187	Catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases. This family includes many uncharacterized bacterial polysaccharide deacetylases. Although their biological function still remains unknown, members in this family show high sequence homology to the catalytic NodB homology domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), which is an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Like SpPgdA, this family is a member of the carbohydrate esterase 4 (CE4) superfamily.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS53029.1|CBM18|CE4	1.70e-209	60	334	105	379
QSS76391.1|CBM18|CE4	3.81e-206	60	334	105	379
QSS58038.1|CBM18|CE4	6.26e-202	60	328	108	376
QKX58110.1|CBM18|CE4	1.80e-111	54	319	92	355
QMW29082.1|CBM18|CE4	2.46e-107	54	318	73	337

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2IW0_A	2.88e-54	99	318	34	247	Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [Colletotrichum lindemuthianum]
7BLY_A	5.55e-50	93	318	27	236	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
2Y8U_A	1.49e-43	84	317	11	229	Chain A, CHITIN DEACETYLASE [Aspergillus nidulans],2Y8U_B Chain B, CHITIN DEACETYLASE [Aspergillus nidulans]
5LFZ_A	6.22e-23	94	307	12	202	T48 deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
2C1G_A	9.62e-19	98	309	227	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|Q6DWK3|CDA_COLLN	2.47e-53	99	318	34	247	Chitin deacetylase OS=Colletotrichum lindemuthianum OX=290576 GN=CDA PE=1 SV=1
sp|A0A1L3THR9|CDA_PESTX	4.11e-48	79	318	12	237	Chitin deacetylase OS=Pestalotiopsis sp. OX=36460 GN=CDA PE=1 SV=1
sp|D4B5F9|PGDA_ARTBC	4.47e-43	86	321	129	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|Q5AQQ0|CDA_EMENI	4.70e-43	81	317	15	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
sp|D4AM78|CDA_ARTBC	5.66e-37	91	318	153	368	Chitin deacetylase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=CDA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000073	0.000000

TMHMM  Annotations     

There is no transmembrane helices in HCDG_04619-t38_1-p1.