CAZyme Information: MGYG000002331_02081

Basic Information

• Species: Vibrio parahaemolyticus
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Vibrio; Vibrio parahaemolyticus
• CAZyme ID: MGYG000002331_02081
• CAZy Family: CBM12
• CAZyme Description: Chitin disaccharide deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
427	MGYG000002331_4|CGC2	47034.11	4.4476

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002331	5262465	Isolate	Bangladesh	Asia

• Gene Location: Start: 429482; End: 430765 Strand: -

Full Sequence      

MKLNKLAIATLVSAALSQYAFAQTDTKGTIYLTFDDGPINASIDVINVLNQEEVKATFYF
NAWHLDGIGDENEDRALEALKLALDSGHIVANHSYDHMVHNCVEEFGPNSAAECNATGDH
QINSYQDPAYDASMFAENLSVLEKYLPNITSYPNYKANEFARLPYTNGWRVTKDFKADGL
CATSDDLKPWEPGYACDTANPSNSVKAAIAVQNILANNGYQTHGWDVDWAPENWGIAMPA
NSLTEAEPFLGYVDSALNTCAPTTINPINSKAQEFPCGTPLHADKVIVLTHEFLFEDGKR
GMGATQNLPKLAKFIQLAKQAGYVFDTMDNYTPNWQVGNNYSAGDYVLHLGTVYQAVTSH
TAQQDWAPSPTSSLWTNADPATNWTQNVSYKQGDVVTYQGLRYLVNVPHVSQADWTPNSQ
NTLFTAL

Enzyme Prediction     

EC	3.1.1.-

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10946	CE4_Mll8295_like	3.82e-76	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	1.19e-15	22	127	1	88	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	2.44e-14	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.
cd10917	CE4_NodB_like_6s_7s	1.19e-12	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.
cd10951	CE4_ClCDA_like	3.42e-12	26	97	6	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGB10915.1	1.81e-292	1	382	1	382
APE82991.1	1.81e-292	1	382	1	382
QRH12406.1	1.81e-292	1	382	1	382
AYF14121.1	1.81e-292	1	382	1	382
BAC60901.1	1.81e-292	1	382	1	382

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3WX7_A	1.22e-276	26	382	1	357	Crystalstructure of COD [Vibrio parahaemolyticus],3WX7_B Crystal structure of COD [Vibrio parahaemolyticus]
4NY2_A	8.26e-233	27	382	6	361	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	6.76e-232	27	382	6	361	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]
5O6Y_A	1.16e-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	1.16e-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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q99PX1	1.04e-292	1	382	1	382	Chitin disaccharide deacetylase OS=Vibrio alginolyticus OX=663 GN=deaA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000275	0.998978	0.000206	0.000194	0.000175	0.000166

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002331_02081.