Species | ||||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; | |||||||||||
CAZyme ID | MGYG000002585_01700 | |||||||||||
CAZy Family | GH9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 13922; End: 16432 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH9 | 115 | 588 | 4.4e-78 | 0.992822966507177 |
CE4 | 617 | 749 | 1e-18 | 0.9230769230769231 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00759 | Glyco_hydro_9 | 2.10e-65 | 123 | 588 | 7 | 374 | Glycosyl hydrolase family 9. |
cd10917 | CE4_NodB_like_6s_7s | 1.17e-29 | 639 | 821 | 19 | 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. |
pfam02927 | CelD_N | 9.00e-29 | 24 | 103 | 2 | 81 | Cellulase N-terminal ig-like domain. |
cd02850 | E_set_Cellulase_N | 1.94e-28 | 24 | 110 | 1 | 86 | N-terminal Early set domain associated with the catalytic domain of cellulase. E or "early" set domains are associated with the catalytic domain of cellulases at the N-terminal end. Cellulases are O-glycosyl hydrolases (GHs) that hydrolyze beta 1-4 glucosidic bonds in cellulose. They are usually categorized into either exoglucanases, which sequentially release terminal sugar units from the cellulose chain, or endoglucanases, which also attack the chain internally. The N-terminal domain of cellulase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others. |
cd10950 | CE4_BsYlxY_like | 1.37e-24 | 616 | 832 | 1 | 186 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT35459.1 | 0.0 | 1 | 836 | 1 | 836 |
QUT98069.1 | 0.0 | 1 | 836 | 1 | 836 |
QPH59586.1 | 0.0 | 1 | 836 | 1 | 836 |
QBJ19309.1 | 0.0 | 1 | 836 | 1 | 836 |
QMI80662.1 | 0.0 | 1 | 836 | 1 | 836 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3X17_A | 1.89e-36 | 22 | 586 | 15 | 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 | 1.48e-27 | 33 | 594 | 2 | 542 | Crystalstructure of Zn-binding triple mutant of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4] |
5U0H_A | 3.28e-24 | 33 | 594 | 2 | 542 | Crystalstructure of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4] |
4CJ0_A | 2.22e-23 | 25 | 589 | 30 | 545 | ChainA, ENDOGLUCANASE D [Acetivibrio thermocellus],4CJ1_A Chain A, ENDOGLUCANASE D [Acetivibrio thermocellus] |
1CLC_A | 2.34e-23 | 25 | 589 | 44 | 559 | ChainA, ENDOGLUCANASE CELD; EC: 3.2.1.4 [Acetivibrio thermocellus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0C2S4 | 1.22e-22 | 25 | 589 | 30 | 545 | Endoglucanase D (Fragment) OS=Acetivibrio thermocellus OX=1515 GN=celD PE=1 SV=1 |
A3DDN1 | 1.33e-22 | 25 | 589 | 54 | 569 | 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 |
A7LXT3 | 4.05e-21 | 25 | 591 | 32 | 578 | Xyloglucan-specific endo-beta-1,4-glucanase BoGH9A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02649 PE=1 SV=1 |
P23658 | 3.10e-19 | 25 | 591 | 4 | 545 | Cellodextrinase OS=Butyrivibrio fibrisolvens OX=831 GN=ced1 PE=1 SV=1 |
A3DCH1 | 5.69e-18 | 25 | 510 | 214 | 737 | Cellulose 1,4-beta-cellobiosidase OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celK PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000313 | 0.998991 | 0.000224 | 0.000159 | 0.000161 | 0.000149 |
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