Species | CAG-279 sp900556245 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-279; CAG-279 sp900556245 | |||||||||||
CAZyme ID | MGYG000002868_01162 | |||||||||||
CAZy Family | GH9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1086; End: 3353 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH9 | 37 | 510 | 1.6e-76 | 0.992822966507177 |
CE4 | 539 | 672 | 8.9e-18 | 0.9307692307692308 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00759 | Glyco_hydro_9 | 5.77e-68 | 45 | 510 | 7 | 374 | Glycosyl hydrolase family 9. |
cd10917 | CE4_NodB_like_6s_7s | 5.85e-31 | 543 | 723 | 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. |
cd10950 | CE4_BsYlxY_like | 9.22e-20 | 538 | 718 | 1 | 158 | 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. |
COG0726 | CDA1 | 2.41e-19 | 481 | 718 | 2 | 222 | Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
pfam01522 | Polysacc_deac_1 | 2.66e-18 | 539 | 671 | 3 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ALJ58617.1 | 0.0 | 1 | 748 | 79 | 827 |
QUT90272.1 | 0.0 | 1 | 748 | 79 | 827 |
QUT35459.1 | 0.0 | 1 | 755 | 79 | 834 |
QUT98069.1 | 0.0 | 1 | 755 | 79 | 834 |
QPH59586.1 | 0.0 | 1 | 755 | 79 | 834 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3X17_A | 1.32e-31 | 5 | 508 | 84 | 551 | Crystalstructure of metagenome-derived glycoside hydrolase family 9 endoglucanase [uncultured bacterium],3X17_B Crystal structure of metagenome-derived glycoside hydrolase family 9 endoglucanase [uncultured bacterium] |
5U2O_A | 3.73e-27 | 8 | 533 | 53 | 553 | Crystalstructure of Zn-binding triple mutant of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4] |
5U0H_A | 8.31e-24 | 8 | 533 | 53 | 553 | Crystalstructure of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4] |
4CJ0_A | 2.86e-17 | 2 | 432 | 79 | 492 | ChainA, ENDOGLUCANASE D [Acetivibrio thermocellus],4CJ1_A Chain A, ENDOGLUCANASE D [Acetivibrio thermocellus] |
1CLC_A | 2.94e-17 | 2 | 432 | 93 | 506 | ChainA, ENDOGLUCANASE CELD; EC: 3.2.1.4 [Acetivibrio thermocellus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0C2S4 | 1.56e-16 | 2 | 432 | 79 | 492 | Endoglucanase D (Fragment) OS=Acetivibrio thermocellus OX=1515 GN=celD PE=1 SV=1 |
A3DDN1 | 1.64e-16 | 2 | 432 | 103 | 516 | Endoglucanase D OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celD PE=1 SV=1 |
P23658 | 2.76e-15 | 2 | 513 | 54 | 545 | Cellodextrinase OS=Butyrivibrio fibrisolvens OX=831 GN=ced1 PE=1 SV=1 |
P14090 | 4.04e-13 | 2 | 517 | 394 | 911 | Endoglucanase C OS=Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547) OX=590998 GN=cenC PE=1 SV=2 |
Q05156 | 3.91e-12 | 2 | 299 | 238 | 537 | Cellulase 1 OS=Streptomyces reticuli OX=1926 GN=cel1 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000067 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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