CAZyme Information: MGYG000004157_00085

Basic Information

• Species: HGM11514 sp900757255
• Lineage: Bacteria; Firmicutes_A; Clostridia; HGM11514; HGM11514; HGM11514; HGM11514 sp900757255
• CAZyme ID: MGYG000004157_00085
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
287	MGYG000004157_2|CGC2	32599.25	8.7668

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004157	2480742	MAG	United Kingdom	Europe

• Gene Location: Start: 13119; End: 13982 Strand: -

Full Sequence      

MKKYTYYSRVRKRRILFKRLRFAGILLCAALLVFGGVKLFGHFRGEASPAFSEQPEVTAE
PSPEISPSPSPVPYSPDRLNGIYQQDGKKIAYLTFDDGPSKGVTEGVLDVLKQYGIKATF
FTLGSQVQKHPELVKRQKEEGHVVGSHGFSHQYKEIYASNECFTADLDQAEAQLKEILGN
DYMKFYRFPGGGYQKSKAPFKEILNAREYYYLDWNCLTDDSMGSYDAEYLKNRLIETAQG
KEKLVILMHDAAAKKTTVEALGPIIEYLKGQGYQFATLQDFIEKKIY

Enzyme Prediction     

No EC number prediction in MGYG000004157_00085.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	85	212	5.9e-28	0.9230769230769231

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10944	CE4_SmPgdA_like	2.32e-79	89	277	1	189	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	1.80e-49	89	269	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.
cd10959	CE4_NodB_like_3	1.22e-44	89	278	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.
COG0726	CDA1	5.14e-42	87	285	63	260	Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
cd10948	CE4_BsPdaA_like	4.37e-41	80	278	30	223	Catalytic NodB homology domain of Bacillus subtilis polysaccharide deacetylase PdaA, and its bacterial homologs. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. This family is represented by Bacillus subtilis pdaA gene encoding polysaccharide deacetylase BsPdaA, which is a member of the carbohydrate esterase 4 (CE4) superfamily. BsPdaA deacetylates peptidoglycan N-acetylmuramic acid (MurNAc) residues to facilitate the formation of muramic delta-lactam, which is required for recognition of germination lytic enzymes. BsPdaA deficiency leads to the absence of muramic delta-lactam residues in the spore cortex. Like other CE4 esterases, BsPdaA consists of a single catalytic NodB homology domain that appears to adopt a deformed (beta/alpha)8 barrel fold with a putative substrate binding groove harboring the majority of the conserved residues. It utilizes a general acid/base catalytic mechanism involving a tetrahedral transition intermediate, where a water molecule functions as the nucleophile tightly associated to the zinc cofactor.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QAT39402.1	1.85e-60	83	279	109	307
ABK60974.1	1.70e-59	48	280	49	272
APQ70984.1	2.82e-59	82	279	72	270
AUN05543.1	2.82e-59	82	279	72	270
APH22826.1	2.82e-59	82	279	72	270

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JMU_A	2.12e-29	87	278	18	213	ChainA, Peptidoglycan N-acetylglucosamine deacetylase [[Eubacterium] rectale ATCC 33656]
2C1G_A	1.02e-27	83	286	230	420	Structureof Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) [Streptococcus pneumoniae R6]
2C1I_A	5.09e-27	83	286	230	420	Structureof Streptococcus pneumoniae peptidoglycan deacetylase (SpPgdA) D 275 N Mutant. [Streptococcus pneumoniae R6]
7FBW_A	8.43e-26	70	285	100	303	ChainA, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
2W3Z_A	3.53e-25	79	279	97	311	Structureof a Streptococcus mutans CE4 esterase [Streptococcus mutans UA159]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8DP63	7.64e-27	83	286	262	452	Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1
Q04729	3.09e-25	77	287	54	259	Uncharacterized 30.6 kDa protein in fumA 3'region OS=Geobacillus stearothermophilus OX=1422 PE=3 SV=1
A0A3Q0NBH7	3.18e-24	88	286	266	450	Peptidoglycan-N-acetylglucosamine deacetylase PgdA OS=Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness) OX=1334565 GN=pgdA PE=1 SV=1
Q8Y9V5	3.18e-24	88	286	266	450	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
A0A0H3GDH9	3.18e-24	88	286	266	450	Peptidoglycan-N-acetylglucosamine deacetylase PgdA OS=Listeria monocytogenes serotype 1/2a (strain 10403S) OX=393133 GN=pgdA PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000039	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
20	42