CAZyme Information: P174DRAFT_439204-t37_1-p1

Basic Information

• Species: Aspergillus novofumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus novofumigatus
• CAZyme ID: P174DRAFT_439204-t37_1-p1
• CAZy Family: GH27
• CAZyme Description: putative polysaccharide deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
261	MSZS01000002|CGC11	28524.31	9.5676

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnovofumigatusIBT16806	11729	1392255	197	11532

• Gene Location: location=MSZS01000002:3233835-3234733(+)

Full Sequence      

MWPLNAYNSSAKQSHPQKLPTPPRIPKTSNSHPPTSDTTPCSTAATAAAENSNASSLLIR
YLQHRYPDVLFHKLVALTIDDAPSQYTREIAATLKAHSASATFFAIGSQIDGDGREAVLA
DLVRGGNELGNHAMRDEPSRALSDEVLAAQIAEVQARISRVYARAGVEEPRVRWFRPGSG
FFSERMRRLVAGMGLKIALGSVYPHDPQVPYAWVNAAHVLSMVRPGSVIICHDRRSWTGP
MLSRGYRVVTLSELVREADGS

Enzyme Prediction     

No EC number prediction in P174DRAFT_439204-t37_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	72	201	3.1e-19	0.9230769230769231

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200581	CE4_NodB_like_2	1.66e-80	73	254	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	1.97e-34	73	238	1	159	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	7.15e-26	73	254	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	1.20e-24	73	251	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	1.52e-23	73	198	7	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
ACQ00943.1|CE4	1.24e-125	56	261	43	263
QMW29882.1|CE4	6.09e-84	56	256	23	236
QMW41954.1|CE4	6.09e-84	56	256	23	236
UDD61559.1|CE4	6.09e-84	56	256	23	236
QRD86297.1|CE4	9.64e-84	56	256	37	250

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7FBW_A	4.36e-15	73	259	117	304	Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
2C71_A	3.75e-11	72	254	4	188	Chain A, Glycoside Hydrolase, Family 11:clostridium Cellulosome Enzyme, Dockerin Type I:polysaccharide [Acetivibrio thermocellus],2C79_A Chain A, GLYCOSIDE HYDROLASE, FAMILY 11:CLOSTRIDIUM CELLULOSOME ENZYME, DOCKERIN TYPE I:POLYSACCHARIDE [Acetivibrio thermocellus]
5LFZ_A	1.05e-06	73	259	25	208	T48 deacetylase [Arthrobacter sp. AW19M34-1],5LGC_A T48 deacetylase with substrate [Arthrobacter sp. AW19M34-1]
7AX7_A	1.29e-06	73	254	4	185	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|P50355|NODB_SINFN	5.39e-11	75	233	20	172	Chitooligosaccharide deacetylase OS=Sinorhizobium fredii (strain NBRC 101917 / NGR234) OX=394 GN=nodB PE=3 SV=2
sp|P24150|NODB_RHILP	9.43e-09	77	233	25	176	Chitooligosaccharide deacetylase OS=Rhizobium leguminosarum bv. phaseoli OX=385 GN=nodB PE=3 SV=1
sp|P02963|NODB_RHIME	3.87e-08	75	233	23	175	Chitooligosaccharide deacetylase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=nodB PE=3 SV=3
sp|P83513|XY11A_PSEXY	1.14e-07	73	254	402	583	Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A PE=1 SV=2
sp|P50352|NODB_BRAEL	1.35e-07	66	233	14	175	Chitooligosaccharide deacetylase OS=Bradyrhizobium elkanii OX=29448 GN=nodB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000068	0.000000

TMHMM  Annotations     

There is no transmembrane helices in P174DRAFT_439204-t37_1-p1.