CAZyme Information: HCAG_07268-t26_1-p1

Basic Information

• Species: Histoplasma capsulatum
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum
• CAZyme ID: HCAG_07268-t26_1-p1
• CAZy Family: GT22
• CAZyme Description: conserved hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
409		46289.33	5.7834

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HcapsulatumNAm1	9402	339724	89	9313

• Gene Location: location=CH476662:1006630-1008004(+)

Full Sequence      

MRFANLVALTNRGICLALFLRSTCASNIPRAQPGEDSVLVIDTFTNGGRNDLDAWHGGGE
DMPVEWGYGFVEFSPTNADQNFHTQLTSTCYDLNPYKDMYLHIVCQGGSHFTVSLSQNNP
QCDAFKNPYPETWDDVEAHRYMKDNDVYIPISHFNIDYTRALSVSFKGFYLDEKLKVSKV
EITATRPENFPAPKKLPTGSLWKRCKRPNSFAFGIDDGSLELGRQMMDILTAEGINATFF
TVGNGLAAPNSGWTNLYKDMLAHGHQVALHSWSHPPYVTSSGEIDEDIIKNIQIVREQLG
FESRYFRPPYGILGARTRQRLARLIKDPQIINWSVDIEDWLWVGSPTPEKQVEAFQRDVD
KGGDLVVMHFLSKDTVMYTKDFIQIARNTGKRIMRVDQCMEDPAAPPLD

Enzyme Prediction     

No EC number prediction in HCAG_07268-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	206	322	1.4e-20	0.8615384615384616

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
213022	CE4_NodB_like_6s_7s	4.07e-41	209	387	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	4.49e-35	205	396	4	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.
223798	CDA1	2.76e-25	206	402	64	259	Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
200578	CE4_CtAXE_like	4.29e-23	212	376	4	157	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.
200582	CE4_NodB_like_3	4.41e-23	211	369	3	154	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
CDP32702.1|CE4	2.44e-25	195	405	34	251
CAP65640.1|CE4	2.44e-25	195	405	34	251
VBB87181.1|CE4	3.37e-25	195	405	34	251
QBZ64293.1|CBM18|CE4	1.36e-24	185	405	35	259
QBZ59347.1|CBM18|CE4	4.61e-23	196	404	59	268

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7BLY_A	1.94e-17	180	405	8	232	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
2IW0_A	4.00e-16	192	402	25	240	Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [Colletotrichum lindemuthianum]
5LFZ_A	1.77e-14	205	398	21	202	T48 deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
7AX7_A	1.27e-08	212	407	7	193	Crystal structure of the Xyl-CE4 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides [uncultured bacterium]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A0H3GDH9|PGDA_LISM4	1.69e-19	162	398	221	444	Peptidoglycan-N-acetylglucosamine deacetylase PgdA OS=Listeria monocytogenes serotype 1/2a (strain 10403S) OX=393133 GN=pgdA PE=2 SV=1
sp|A0A3Q0NBH7|PGDA_LISMG	1.69e-19	162	398	221	444	Peptidoglycan-N-acetylglucosamine deacetylase PgdA OS=Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness) OX=1334565 GN=pgdA PE=1 SV=1
sp|Q8Y9V5|PGDA_LISMO	1.69e-19	162	398	221	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
sp|A0A1L3THR9|CDA_PESTX	1.33e-16	196	405	26	233	Chitin deacetylase OS=Pestalotiopsis sp. OX=36460 GN=CDA PE=1 SV=1
sp|Q6DWK3|CDA_COLLN	1.01e-15	192	402	25	240	Chitin deacetylase OS=Colletotrichum lindemuthianum OX=290576 GN=CDA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.052887	0.947083	CS pos: 23-24. Pr: 0.8133

TMHMM  Annotations     

There is no transmembrane helices in HCAG_07268-t26_1-p1.