CAZyme Information: MGYG000003702_02535

Basic Information

• Species: Eisenbergiella sp900066775
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900066775
• CAZyme ID: MGYG000003702_02535
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
279	MGYG000003702_19|CGC1	31518.85	6.3304

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003702	3523328	Isolate	China	Asia

• Gene Location: Start: 41424; End: 42263 Strand: -

Full Sequence      

MIRDFVHLIQNKLRHYAVFPSLHSLSRSSAFQTALFLLGVLAFARACIFLAPPSVTALAS
ASVNGTFMPICRVETDQKKVALTFNCTYSAQDLHQLLEILKEKNVHATFFVSDTWAKNYP
KLLCTIHNAGHDIGGLWTTQASLSIREQTLTLENLTQRIDRLTDSETTLFRFEDGNYDNS
AIRLIQEAGGYPVQWNINSMDWKDYGAQDILHRILNSRQLQNGSILLFHAGTVYTAQALP
DLIDNLEDQGYQPVPISELIWKHSYYMDADGVQIPKTEP

Enzyme Prediction     

No EC number prediction in MGYG000003702_02535.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	74	189	3.1e-17	0.8923076923076924

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02764	spore_ybaN_pdaB	2.01e-52	73	260	1	191	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]
cd10949	CE4_BsPdaB_like	1.43e-43	75	260	1	190	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.
cd10917	CE4_NodB_like_6s_7s	1.64e-40	78	246	1	170	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.
cd10950	CE4_BsYlxY_like	5.30e-39	75	260	3	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.
cd10948	CE4_BsPdaA_like	2.45e-28	74	251	36	218	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
QDW74975.1	1.61e-59	60	274	37	254
QBF74253.1	4.56e-58	60	274	37	254
QRO37510.1	4.56e-58	60	274	37	254
QEK18798.1	1.29e-57	60	274	37	254
QYX27773.1	3.64e-57	60	274	37	254

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4M1B_A	5.25e-26	70	260	49	243	StructuralDetermination of BA0150, a Polysaccharide Deacetylase from Bacillus anthracis [Bacillus anthracis],4M1B_B Structural Determination of BA0150, a Polysaccharide Deacetylase from Bacillus anthracis [Bacillus anthracis]
7FBW_A	9.21e-22	78	262	117	302	ChainA, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
7BKF_A	1.22e-20	69	260	77	268	ChainA, Putative polysaccharide deacetylase [Bacillus anthracis]
6HM9_A	1.59e-20	69	260	76	267	Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme with restored enzymatic activity. [Bacillus anthracis]
2J13_A	3.45e-20	74	260	51	242	Structureof a family 4 carbohydrate esterase from Bacillus anthracis [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P50865	1.13e-22	70	260	49	243	Probable polysaccharide deacetylase PdaB OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaB PE=3 SV=2
O34798	1.17e-16	73	259	273	457	Peptidoglycan-N-acetylmuramic acid deacetylase PdaC OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaC PE=1 SV=1
P50850	1.69e-16	69	260	121	312	Uncharacterized protein YlxY OS=Bacillus subtilis (strain 168) OX=224308 GN=ylxY PE=3 SV=2
Q04729	8.10e-16	74	265	63	259	Uncharacterized 30.6 kDa protein in fumA 3'region OS=Geobacillus stearothermophilus OX=1422 PE=3 SV=1
O34928	1.25e-13	75	262	63	255	Peptidoglycan-N-acetylmuramic acid deacetylase PdaA OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaA 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
0.994038	0.005820	0.000043	0.000018	0.000014	0.000053

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003702_02535.