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CAZyme Information: MGYG000002311_00941
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Vibrio cholerae | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Vibrio; Vibrio cholerae | |||||||||||
| CAZyme ID | MGYG000002311_00941 | |||||||||||
| CAZy Family | CE4 | |||||||||||
| CAZyme Description | Chitin disaccharide deacetylase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1033127; End: 1034410 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd10946 | CE4_Mll8295_like | 7.68e-90 | 28 | 331 | 1 | 217 | Putative catalytic NodB homology domain of uncharacterized Mll8295 protein encoded from Rhizobium loti and its bacterial homologs. This family is represented by a putative polysaccharide deacetylase Mll8295 encoded from Rhizobium loti. Although its biological function still remains unknown, Mll8295 shows high sequence homology to the catalytic 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. Both Mll8295 and SpPgdA belong to the carbohydrate esterase 4 (CE4) superfamily. This family also includes many uncharacterized bacterial polysaccharide deacetylases. |
| pfam01522 | Polysacc_deac_1 | 7.03e-19 | 22 | 168 | 1 | 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. |
| cd10944 | CE4_SmPgdA_like | 6.89e-15 | 29 | 97 | 2 | 62 | 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. |
| cd10951 | CE4_ClCDA_like | 1.16e-13 | 28 | 97 | 8 | 73 | 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. |
| cd10917 | CE4_NodB_like_6s_7s | 1.25e-13 | 28 | 97 | 1 | 63 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| APF71342.1 | 5.43e-294 | 1 | 383 | 1 | 383 |
| AWA78647.1 | 5.43e-294 | 1 | 383 | 1 | 383 |
| APF59879.1 | 5.43e-294 | 1 | 383 | 1 | 383 |
| BAP02716.1 | 5.43e-294 | 1 | 383 | 1 | 383 |
| AFC58071.1 | 5.43e-294 | 1 | 383 | 1 | 383 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4NY2_A | 3.60e-280 | 23 | 383 | 2 | 362 | Structureof Vibrio cholerae chitin de-N-acetylase in complex with acetate ion (ACT) in P 21 [Vibrio cholerae O1 str. NHCC-010F],4NY2_B Structure of Vibrio cholerae chitin de-N-acetylase in complex with acetate ion (ACT) in P 21 [Vibrio cholerae O1 str. NHCC-010F],4NYU_A Structure of Vibrio cholerae chitin de-N-acetylase in complex with acetate ion (ACT) in C 2 2 21 [Vibrio cholerae O1 str. NHCC-010F],4NYY_A Structure of Vibrio cholerae chitin de-N-acetylase in complex with acetate ion (ACT) in P 2 21 21 [Vibrio cholerae O1 str. NHCC-010F],4NYY_B Structure of Vibrio cholerae chitin de-N-acetylase in complex with acetate ion (ACT) in P 2 21 21 [Vibrio cholerae O1 str. NHCC-010F],4NYY_C Structure of Vibrio cholerae chitin de-N-acetylase in complex with acetate ion (ACT) in P 2 21 21 [Vibrio cholerae O1 str. NHCC-010F],4NYY_D Structure of Vibrio cholerae chitin de-N-acetylase in complex with acetate ion (ACT) in P 2 21 21 [Vibrio cholerae O1 str. NHCC-010F],4NZ4_A Structure of Vibrio cholerae chitin de-N-acetylase in complex with 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE (NDG) and zinc ion [Vibrio cholerae O1 str. NHCC-010F],4NZ4_B Structure of Vibrio cholerae chitin de-N-acetylase in complex with 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE (NDG) and zinc ion [Vibrio cholerae O1 str. NHCC-010F],4NZ5_A Structure of Vibrio cholerae chitin de-N-acetylase in complex with 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE (NDG) and cadmium ion [Vibrio cholerae O1 str. NHCC-010F],4NZ5_B Structure of Vibrio cholerae chitin de-N-acetylase in complex with 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE (NDG) and cadmium ion [Vibrio cholerae O1 str. NHCC-010F] |
| 4NZ1_A | 2.95e-279 | 23 | 383 | 2 | 362 | Structureof Vibrio cholerae chitin de-N-acetylase in complex with DI(N-ACETYL-D-GLUCOSAMINE) (CBS) in P 21 [Vibrio cholerae O1 str. NHCC-010F],4NZ1_B Structure of Vibrio cholerae chitin de-N-acetylase in complex with DI(N-ACETYL-D-GLUCOSAMINE) (CBS) in P 21 [Vibrio cholerae O1 str. NHCC-010F],4NZ3_A Structure of Vibrio cholerae chitin de-N-acetylase in complex with DI(N-ACETYL-D-GLUCOSAMINE) (CBS) in P 21 21 21 [Vibrio cholerae O1 str. NHCC-010F],4NZ3_B Structure of Vibrio cholerae chitin de-N-acetylase in complex with DI(N-ACETYL-D-GLUCOSAMINE) (CBS) in P 21 21 21 [Vibrio cholerae O1 str. NHCC-010F],4OUI_A Structure of Vibrio cholerae chitin de-N-acetylase in complex with TRIACETYLCHITOTRIOSE (CTO) [Vibrio cholerae O1 str. NHCC-010F],4OUI_B Structure of Vibrio cholerae chitin de-N-acetylase in complex with TRIACETYLCHITOTRIOSE (CTO) [Vibrio cholerae O1 str. NHCC-010F] |
| 3WX7_A | 5.14e-232 | 27 | 382 | 2 | 357 | Crystalstructure of COD [Vibrio parahaemolyticus],3WX7_B Crystal structure of COD [Vibrio parahaemolyticus] |
| 5O6Y_A | 1.56e-06 | 19 | 97 | 12 | 83 | Crystalstructure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579] |
| 5O6Y_B | 1.56e-06 | 19 | 97 | 12 | 83 | Crystalstructure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579],5O6Y_C Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579],5O6Y_D 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 download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q99PX1 | 1.49e-239 | 1 | 382 | 1 | 382 | Chitin disaccharide deacetylase OS=Vibrio alginolyticus OX=663 GN=deaA PE=1 SV=1 |
| D4B5F9 | 3.44e-07 | 18 | 97 | 139 | 213 | Probable peptidoglycan-N-acetylglucosamine deacetylase ARB_03699 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03699 PE=1 SV=2 |
| D4AM78 | 1.61e-06 | 25 | 97 | 165 | 232 | Chitin deacetylase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=CDA PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000289 | 0.998935 | 0.000214 | 0.000196 | 0.000179 | 0.000168 |