CAZyme Information: RAK79910.1

Basic Information

• Species: Aspergillus fijiensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fijiensis
• CAZyme ID: RAK79910.1
• CAZy Family: GH75
• CAZyme Description: putative polysaccharide deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
262	KZ824631|CGC5	29431.45	9.9638

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfijiensisCBS313.89	12336	1448319	318	12018

• Gene Location: location=KZ824631:305791-306630(-)

Full Sequence      

MALLTLCLLLTLLILLPAYTIYRPPNLLIRYFQHRWPDALFHVPLPASAPPTIALTIDDS
PSTFTAQILEILRENDARATFFVIGAQIPAPGVGPRGGNGEAMLRELVREGMELGNHAMS
DRPSRDLSDAVLEAEVRGVQGWLERVEDLVFPAKAKYKWFRPGSGFFSDRMRVLIRKLGL
RIALGSVYPHDAQINWPRVNAWHILSMVRSGSVIVCHDRRGWTVPMLKLVVPELKRRGFR
VVTLSELVELGEQSQLPKQISA

Enzyme Prediction     

No EC number prediction in RAK79910.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	49	186	1.8e-20	0.9307692307692308

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200581	CE4_NodB_like_2	2.96e-81	51	247	1	190	Catalytic NodB homology domain of uncharacterized chitin deacetylases and hypothetical proteins. This family includes some uncharacterized chitin deacetylases and hypothetical proteins, mainly from eukaryotes. Although their biological function is unknown, members in this family show high sequence homology to the catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41), which catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. Like ClCDA, this family is a member the carbohydrate esterase 4 (CE4) superfamily.
213022	CE4_NodB_like_6s_7s	1.91e-40	51	235	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.
200578	CE4_CtAXE_like	1.36e-35	51	247	1	180	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	1.63e-32	51	244	1	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.
396211	Polysacc_deac_1	1.00e-29	50	183	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
QMW29882.1|CE4	9.26e-96	9	254	6	241
QMW41954.1|CE4	9.26e-96	9	254	6	241
UDD61559.1|CE4	9.26e-96	9	254	6	241
QRD86297.1|CE4	1.48e-95	9	254	20	255
BAE60108.1|CE4	1.48e-95	9	254	20	255

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7FBW_A	8.43e-19	53	249	119	301	Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
2J13_A	4.00e-14	53	252	57	246	Structure of a family 4 carbohydrate esterase from Bacillus anthracis [Bacillus anthracis str. Ames]
2C1G_A	7.28e-14	53	248	238	416	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) [Streptococcus pneumoniae R6]
6HM9_A	7.89e-14	53	249	87	268	Crystal structure of a BA3943 mutant,a CE4 family pseudoenzyme with restored enzymatic activity. [Bacillus anthracis]
7AX7_A	8.58e-14	53	249	6	187	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|Q81AF4|PGDA3_BACCR	1.69e-23	53	248	24	209	Peptidoglycan-N-acetylglucosamine deacetylase BC_3618 OS=Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711) OX=226900 GN=BC_3618 PE=1 SV=1
sp|P50355|NODB_SINFN	1.39e-15	38	246	5	213	Chitooligosaccharide deacetylase OS=Sinorhizobium fredii (strain NBRC 101917 / NGR234) OX=394 GN=nodB PE=3 SV=2
sp|P83513|XY11A_PSEXY	1.02e-13	53	250	404	586	Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A PE=1 SV=2
sp|P04675|NODB_BRASP	1.89e-13	52	247	22	218	Chitooligosaccharide deacetylase OS=Bradyrhizobium sp. (strain ANU 289) OX=186901 GN=nodB PE=3 SV=2
sp|Q8DP63|PGDA_STRR6	3.98e-13	53	248	270	448	Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.968237	0.031784

TMHMM  Annotations     

Start	End
2	21