CAZyme Information: MGYG000004439_01455

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; UMGS1810; UMGS1810
• CAZyme ID: MGYG000004439_01455
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
191	MGYG000004439_67|CGC1	21614.71	6.841

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004439	2174785	MAG	Israel	Asia

• Gene Location: Start: 9478; End: 10053 Strand: +

Full Sequence      

MKLYVVTAKKLLGNLLVAAALLTVVGLNYTQTKSVFKNEASRKLPIYNVEREDKVCAISF
DAAWGNEDTHDLISILEKYKVKATFFVVGDWVDRYPESVKELHDAGHDVMNHSNTHPHMT
QISKEKMISEVTECDNKIEKITGVKPNLFRPPYGDYNDNVVTNLKEIGHYTIQWDVDTLA
AVGKPTRTVTF

Enzyme Prediction     

No EC number prediction in MGYG000004439_01455.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	48	169	9.3e-35	0.9153846153846154

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10917	CE4_NodB_like_6s_7s	4.91e-53	54	179	1	126	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.
TIGR02764	spore_ybaN_pdaB	1.13e-51	49	179	1	131	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]
cd10950	CE4_BsYlxY_like	7.94e-46	51	179	3	131	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.
pfam01522	Polysacc_deac_1	4.61e-43	48	172	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.
cd10954	CE4_CtAXE_like	6.86e-40	54	179	1	123	Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its bacterial homologs. This family is represented by Clostridium thermocellum acetylxylan esterase (CtAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. CtAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan, as a consequence of deacetylation. CtAXE is a monomeric protein containing a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases. However, due to differences in the topography of the substrate-binding groove, the chemistry of the active center, and metal ion coordination, CtAXE has different metal ion preference and lacks activity on N-acetyl substrates. It is significantly activated by Co2+. Moreover, CtAXE displays distinctly different ligand coordination to the metal ion, utilizing an aspartate, a histidine, and four water molecules, as opposed to the conserved His-His-Asp zinc-binding triad of other CE4 esterases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANU39676.1	3.98e-66	42	190	40	188
QQR07498.1	3.98e-66	42	190	40	188
QIA29235.1	3.98e-66	42	190	40	188
CDZ25029.1	5.08e-65	41	189	43	191
QNL43472.1	5.72e-63	1	190	1	188

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6HM9_A	6.24e-26	45	179	76	210	Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme with restored enzymatic activity. [Bacillus anthracis]
6HPA_A	2.19e-25	45	179	77	211	Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme [Bacillus anthracis]
7BKF_A	1.38e-24	45	179	77	211	ChainA, Putative polysaccharide deacetylase [Bacillus anthracis]
6H8L_A	2.59e-24	49	177	5	130	Structureof peptidoglycan deacetylase PdaC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],6H8L_B Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
6H8N_A	1.99e-23	49	177	5	130	Structureof peptidoglycan deacetylase PdaC from Bacillus subtilis - mutant D285S [Bacillus subtilis subsp. subtilis str. 168],6H8N_B Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis - mutant D285S [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P50850	2.45e-26	29	179	105	255	Uncharacterized protein YlxY OS=Bacillus subtilis (strain 168) OX=224308 GN=ylxY PE=3 SV=2
O34798	3.78e-22	49	177	273	398	Peptidoglycan-N-acetylmuramic acid deacetylase PdaC OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaC PE=1 SV=1
O34928	1.19e-20	52	176	64	189	Peptidoglycan-N-acetylmuramic acid deacetylase PdaA OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaA PE=1 SV=1
Q81EK9	2.81e-20	57	190	84	217	Peptidoglycan-N-acetylglucosamine deacetylase BC_1960 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_1960 PE=1 SV=1
Q8DP63	5.11e-19	47	179	261	390	Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 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
0.804966	0.186597	0.002087	0.000951	0.000607	0.004802

TMHMM  Annotations     

start	end
12	29