Species | Bacillus_A paranthracis | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A paranthracis | |||||||||||
CAZyme ID | MGYG000002283_02269 | |||||||||||
CAZy Family | CE4 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2174968; End: 2176950 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE4 | 472 | 593 | 5.3e-32 | 0.9076923076923077 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd10917 | CE4_NodB_like_6s_7s | 6.71e-65 | 474 | 646 | 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. |
TIGR02764 | spore_ybaN_pdaB | 3.00e-61 | 473 | 659 | 5 | 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] |
cd10950 | CE4_BsYlxY_like | 5.72e-60 | 473 | 659 | 5 | 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. |
cd10954 | CE4_CtAXE_like | 1.08e-59 | 474 | 658 | 1 | 180 | 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. |
COG4641 | COG4641 | 5.54e-53 | 1 | 333 | 32 | 372 | Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ASI78850.1 | 0.0 | 1 | 660 | 1 | 660 |
QWI25601.1 | 0.0 | 1 | 660 | 1 | 660 |
QED49911.1 | 0.0 | 1 | 660 | 1 | 660 |
QWI25600.1 | 1.74e-139 | 1 | 394 | 1 | 394 |
QED49910.1 | 2.77e-138 | 1 | 394 | 1 | 394 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7FBW_A | 2.06e-38 | 453 | 660 | 96 | 301 | ChainA, Predicted xylanase/chitin deacetylase [Caldanaerobacter subterraneus subsp. tengcongensis MB4] |
6HM9_A | 1.70e-36 | 453 | 660 | 61 | 268 | Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme with restored enzymatic activity. [Bacillus anthracis] |
6HPA_A | 5.28e-36 | 453 | 660 | 62 | 269 | Crystalstructure of a BA3943 mutant,a CE4 family pseudoenzyme [Bacillus anthracis] |
7BKF_A | 3.17e-35 | 453 | 660 | 62 | 269 | ChainA, Putative polysaccharide deacetylase [Bacillus anthracis] |
6H8L_A | 3.40e-35 | 473 | 660 | 9 | 191 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O31681 | 1.17e-127 | 1 | 392 | 1 | 386 | Spore protein YkvP OS=Bacillus subtilis (strain 168) OX=224308 GN=ykvP PE=2 SV=1 |
P50850 | 1.07e-36 | 416 | 660 | 50 | 313 | Uncharacterized protein YlxY OS=Bacillus subtilis (strain 168) OX=224308 GN=ylxY PE=3 SV=2 |
O34798 | 7.19e-34 | 406 | 660 | 214 | 459 | Peptidoglycan-N-acetylmuramic acid deacetylase PdaC OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaC PE=1 SV=1 |
P50865 | 6.23e-32 | 466 | 659 | 49 | 243 | Probable polysaccharide deacetylase PdaB OS=Bacillus subtilis (strain 168) OX=224308 GN=pdaB PE=3 SV=2 |
Q8DP63 | 2.90e-31 | 454 | 659 | 246 | 448 | Peptidoglycan-N-acetylglucosamine deacetylase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=pgdA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000070 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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