CAZyme Information: MGYG000000157_00343

Basic Information

• Species: Paraclostridium sordellii
• Lineage: Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Paraclostridium; Paraclostridium sordellii
• CAZyme ID: MGYG000000157_00343
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
251		28805.51	9.4188

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000157	3456733	Isolate	China	Asia

• Gene Location: Start: 73856; End: 74611 Strand: -

Full Sequence      

MIMMVLNKKKLKKIFIGILVIILAILGFLFVNRNNDKPTLNMFYKASEPYYNGNKTNSGR
VAISCNVDLGWESEYIEKILKVLDEKKAKITFAVTGRWAEENPEFLLEIQKKGHEIANHG
YKHLDYGTLDYDKNYEQIKTSKKIIDEIIKTQTKFFQAPGGSFNKDTVKAAIDLGYIPYK
WDIDTIDWKNRQEPEVIIKRVKSKDMKDSSIILMHPTHASAEGIDDIIEIIESKGLKPGK
LSDVFDVKKTI

Enzyme Prediction     

No EC number prediction in MGYG000000157_00343.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	57	176	8.6e-24	0.9

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10950	CE4_BsYlxY_like	2.03e-71	55	245	2	188	Putative catalytic NodB homology domain of uncharacterized protein YlxY from Bacillus subtilis 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 putative polysaccharide deacetylase BsYlxY, encoded by the ylxY gene, which is a member of the carbohydrate esterase 4 (CE4) superfamily. Although its biological function still remains unknown, BsYlxY shows high sequence homology to the catalytic domain of Bacillus subtilis pdaB gene encoding a putative polysaccharide deacetylase (BsPdaB), which is essential for the maintenance of spores after the late stage of sporulation and is highly conserved in spore-forming bacteria. However, disruption of the ylxY gene in B. subtilis did not cause any sporulation defect. Moreover, the Asp residue in the classical His-His-Asp zinc-binding motif of CE4 esterases is mutated to a Val residue in this family. Other catalytically relevant residues of CE4 esterases are also not conserved, which suggest that members of this family may be inactive.
TIGR02764	spore_ybaN_pdaB	3.04e-45	56	215	3	158	polysaccharide deacetylase family sporulation protein PdaB. This model describes the YbaN protein family, also called PdaB and SpoVIE, of Gram-positive bacteria. Although ybaN null mutants have only a mild sporulation defect, ybaN/ytrI double mutants show drastically reducted sporulation efficiencies. This synthetic defect suggests the role of this sigmaE-controlled gene in sporulation had been masked by functional redundancy. Members of this family are homologous to a characterized polysaccharide deacetylase; the exact function this protein family is unknown. [Cellular processes, Sporulation and germination]
cd10917	CE4_NodB_like_6s_7s	6.79e-45	59	220	1	158	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.
COG0726	CDA1	5.35e-38	1	218	5	225	Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
cd10949	CE4_BsPdaB_like	2.56e-32	56	215	1	157	Putative catalytic NodB homology domain of Bacillus subtilis putative polysaccharide deacetylase PdaB, 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 the putative polysaccharide deacetylase PdaB encoded by the pdaB gene on sporulation of Bacillus subtilis. Although its biochemical properties remain to be determined, the PdaB (YbaN) protein is essential for maintaining spores after the late stage of sporulation and is highly conserved in spore-forming bacteria. The glycans of the spore cortex may be candidate PdaB substrates. Based on sequence similarity, the family members are classified as carbohydrate esterase 4 (CE4) superfamily members. However, the classical His-His-Asp zinc-binding motif of CE4 esterases is missing in this family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOX87720.1	3.72e-101	1	245	1	246
QUP85098.1	3.72e-101	1	245	1	246
QQY59899.1	3.72e-101	1	245	1	246
QQY62766.1	3.72e-101	1	245	1	246
QPK95971.1	3.72e-101	1	245	1	246

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6HPA_A	6.66e-39	38	249	66	272	Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme [Bacillus anthracis]
6HM9_A	2.09e-38	38	249	65	271	Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme with restored enzymatic activity. [Bacillus anthracis]
7BKF_A	3.24e-38	38	249	66	272	ChainA, Putative polysaccharide deacetylase [Bacillus anthracis]
2J13_A	1.41e-19	68	244	62	241	Structureof a family 4 carbohydrate esterase from Bacillus anthracis [Bacillus anthracis str. Ames]
3RXZ_A	2.84e-08	76	177	64	165	Crystalstructure of putative polysaccharide deacetylase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155],3RXZ_B Crystal structure of putative polysaccharide deacetylase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155],3RXZ_C Crystal structure of putative polysaccharide deacetylase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155],3RXZ_D Crystal structure of putative polysaccharide deacetylase from Mycobacterium smegmatis [Mycolicibacterium smegmatis MC2 155]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P50850	8.74e-36	37	246	109	313	Uncharacterized protein YlxY OS=Bacillus subtilis (strain 168) OX=224308 GN=ylxY PE=3 SV=2
P50355	6.96e-12	55	215	12	171	Chitooligosaccharide deacetylase OS=Sinorhizobium fredii (strain NBRC 101917 / NGR234) OX=394 GN=nodB PE=3 SV=2
P02963	3.51e-11	78	215	38	174	Chitooligosaccharide deacetylase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=nodB PE=3 SV=3
P50352	3.61e-11	79	222	39	181	Chitooligosaccharide deacetylase OS=Bradyrhizobium elkanii OX=29448 GN=nodB PE=3 SV=1
P04339	1.69e-10	78	215	38	174	Chitooligosaccharide deacetylase OS=Rhizobium leguminosarum bv. viciae OX=387 GN=nodB PE=3 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
0.994146	0.005500	0.000170	0.000021	0.000013	0.000165

TMHMM  Annotations     

start	end
13	32