CAZyme Information: RQM09665.1

Basic Information

• Species: Peronospora effusa
• Lineage: Oomycota; NA; ; Peronosporaceae; Peronospora; Peronospora effusa
• CAZyme ID: RQM09665.1
• CAZy Family: AA17|AA17
• CAZyme Description: NodB homology domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A425BY24]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
316		35552.03	8.0800

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PeffusaR13	8603	N/A	0	8603

• Gene Location: location=QKXF01000678:30003-30953(+)

Full Sequence      

MKSRLSSVVLYSVATLPLPSSAGLVDFIDAVSMSMTATIVSIFLLLITSLFLLSVYLLPD
WLLRCLEWNSHPSVLWSARTSSRVCSLTIDDAPSSSTPAILDILGKYNVKATFFIISDHI
PGNEEVLRRIVQEGHVLANHLTEDRASILDELHVFEKKLQECDRAINKFQPTEREMSLQE
TLQPRREEKKMDTVQLVADVTDKMREATGSRSKWMRPASGWFTTPMRKITARHGYRICLG
SVYPHDAQIRSETINSMHLQTRTTCGSVIIVHDRSWTIGVLKTALPVLTSKFTFVSLDKL
VSYHEGKSTKDDEAGK

Enzyme Prediction     

No EC number prediction in RQM09665.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	79	240	4.3e-19	0.9384615384615385

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200581	CE4_NodB_like_2	2.49e-85	83	300	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	2.24e-32	83	288	1	166	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.
200569	CE4_SmPgdA_like	5.57e-25	87	286	5	174	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.
396211	Polysacc_deac_1	6.40e-24	80	236	4	122	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	9.69e-24	87	297	5	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
ACK74140.1|CE4	2.83e-40	59	308	23	237
CAK43258.1|CE4	1.41e-37	55	313	63	309
ACF22102.1|CE4	1.31e-35	69	288	50	294
EAA66033.1|CE4	1.31e-35	69	288	50	294
AFZ46169.1|CE4	1.31e-34	56	300	28	240

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C1G_A	2.77e-17	83	302	236	417	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) [Streptococcus pneumoniae R6]
2C1I_A	1.25e-16	83	302	236	417	Structure of Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) D 275 N Mutant. [Streptococcus pneumoniae R6]
7BLY_A	2.98e-12	80	148	37	104	Chain A, Aspergillus niger contig An12c0130, genomic contig [Aspergillus niger CBS 513.88]
2Y8U_A	6.60e-10	80	148	30	97	Chain A, CHITIN DEACETYLASE [Aspergillus nidulans],2Y8U_B Chain B, CHITIN DEACETYLASE [Aspergillus nidulans]
5O6Y_A	3.38e-09	67	140	5	79	Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8DP63|PGDA_STRR6	1.60e-16	83	302	268	449	Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1
sp|Q81AF4|PGDA3_BACCR	9.32e-11	74	303	13	211	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|P02963|NODB_RHIME	9.87e-11	80	166	18	105	Chitooligosaccharide deacetylase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=nodB PE=3 SV=3
sp|Q8Y9V5|PGDA_LISMO	1.30e-10	78	300	262	445	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|A0A3Q0NBH7|PGDA_LISMG	1.30e-10	78	300	262	445	Peptidoglycan-N-acetylglucosamine deacetylase PgdA OS=Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness) OX=1334565 GN=pgdA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.835186	0.164834

TMHMM  Annotations     

Start	End
7	25
35	57