CAZyme Information: EFQ29632.1

Basic Information

• Species: Colletotrichum graminicola
• Lineage: Ascomycota; Sordariomycetes; ; Glomerellaceae; Colletotrichum; Colletotrichum graminicola
• CAZyme ID: EFQ29632.1
• CAZy Family: CE9
• CAZyme Description: NodB homology domain-containing protein [Source:UniProtKB/TrEMBL;Acc:E3QFJ4]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
761	GG697345|CGC2	81837.73	6.6079

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CgraminicolaM1-001	12400	645133	380	12020

• Gene Location: location=GG697345:702784-705198(+)

Full Sequence      

MLHLKVRSLLATAYTAVVAAAVCSSDLLVDDLSNSFSTNRNNLGSWTSDDGSMASISASG
GILSFTPKSGAYFYETLPCQALQTDSYTHVQLDIKAPVSGAAFTTELSWASSCSATTTTK
TAFRVTSLTGGWQTLRIPLSSFTGANLNAALSVVIGSFSSTQQWQLDKVQFVCGQTTTTS
AGITSTQAPTIPASSTTPSAPPSSCSPLLVDDWASQSRLSFLAYNALLLPTGDDGTMQSV
VVDNHHVTLTPKSTSSYFYSQVGCVDATRYGGISLWVKAPAGTTFRIELSSKTTCDGAAT
ASSTQTTAQLGWTFDGTEKLYSFSWSKFSGINLTKLRSIVISAPNQPLNLGPLAFYCGST
PSGWIVPSASSPAAPTQTVEAPAATASAFIVDAFDSPSTNSLGFWHGGEDLSLSWGQNRL
TIVASASDYAFTTLMSNGCRDLRSHSGSYLHIAYSGHTRFSVSLQQHNSQCNSGVAPYPE
TRDSLEAGRYATGNDIYIPISHFDINLQRVSSVAIRGMYSSEPVILSKIEMVPSIPSGVS
IPRKLPSGTLVFSCTRPNSFAFGIDDGNPRYAARLAEMIREAGIKVTFFAVGAVLENNAT
GMADLYRQLRSEGHQIALHSYTHPRMEGLASTASIDWEYNEDYRVMTGIFGEKSNYFRPP
YGVEGARMRQRWAAASGAAKAYLINWSVDVQDWLWAETSTPEKQVDAFKADVAKGGNLVV
MHFSYNSTVNYFPEFIRQAKATGKQIMRIDQCMEDPNAPPL

Enzyme Prediction     

No EC number prediction in EFQ29632.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	555	670	4.8e-18	0.8384615384615385

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
213022	CE4_NodB_like_6s_7s	4.37e-41	558	740	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	7.07e-30	551	743	1	191	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.
200578	CE4_CtAXE_like	3.74e-26	561	746	4	174	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	4.33e-24	560	743	3	181	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.
200569	CE4_SmPgdA_like	8.71e-24	564	743	7	184	Catalytic NodB homology domain of Streptococcus mutans polysaccharide deacetylase PgdA, Bacillus subtilis YheN, and similar proteins. This family is represented by a putative polysaccharide deacetylase PgdA from the oral pathogen Streptococcus mutans (SmPgdA) and Bacillus subtilis YheN (BsYheN), which are members of the carbohydrate esterase 4 (CE4) superfamily. SmPgdA is an extracellular metal-dependent polysaccharide deacetylase with a typical CE4 fold, with metal bound to a His-His-Asp triad. It possesses de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. SmPgdA plays a role in tuning cell surface properties and in interactions with (salivary) agglutinin, an essential component of the innate immune system, most likely through deacetylation of an as-yet-unidentified polysaccharide. SmPgdA shows significant homology to the catalytic domains of peptidoglycan deacetylases from Streptococcus pneumoniae (SpPgdA) and Listeria monocytogenes (LmPgdA), both of which are involved in the bacterial defense mechanism against human mucosal lysozyme. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. The biological function of BsYheN is still unknown. This family also includes many uncharacterized polysaccharide deacetylases mainly found in bacteria.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPC59605.1|CE4	3.22e-23	543	756	26	234
QPC70944.1|CE4	8.01e-23	543	756	26	234
CEI62102.1|CE4	1.47e-22	543	756	26	234
CZS81661.1|CE4	1.66e-21	543	756	26	234
CEF78366.1|CE4	1.66e-21	543	756	26	234

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7BLY_A	8.29e-21	526	758	5	232	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
2C1G_A	3.19e-15	561	753	239	416	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) [Streptococcus pneumoniae R6]
2IW0_A	9.16e-15	543	755	27	240	Structure of the chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum [Colletotrichum lindemuthianum]
2C1I_A	1.33e-14	561	753	239	416	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) D 275 N Mutant. [Streptococcus pneumoniae R6]
7FBW_A	1.88e-14	561	754	120	301	Chain A, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1L3THR9|CDA_PESTX	2.91e-17	545	758	26	233	Chitin deacetylase OS=Pestalotiopsis sp. OX=36460 GN=CDA PE=1 SV=1
sp|D4AM78|CDA_ARTBC	1.34e-16	541	758	151	364	Chitin deacetylase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=CDA PE=3 SV=1
sp|Q8DP63|PGDA_STRR6	1.95e-14	561	753	271	448	Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1
sp|Q6DWK3|CDA_COLLN	5.76e-14	543	755	27	240	Chitin deacetylase OS=Colletotrichum lindemuthianum OX=290576 GN=CDA PE=1 SV=1
sp|Q5AQQ0|CDA_EMENI	1.59e-13	543	755	25	230	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
0.741094	0.258913

TMHMM  Annotations     

There is no transmembrane helices in EFQ29632.1.