Species | Parabacteroides sp900770835 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900770835 | |||||||||||
CAZyme ID | MGYG000003521_01139 | |||||||||||
CAZy Family | GH9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1530; End: 4139 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH9 | 146 | 619 | 9.2e-75 | 0.992822966507177 |
CE4 | 651 | 780 | 1.5e-16 | 0.9 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00759 | Glyco_hydro_9 | 2.54e-65 | 154 | 619 | 7 | 374 | Glycosyl hydrolase family 9. |
cd10917 | CE4_NodB_like_6s_7s | 1.11e-27 | 652 | 852 | 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. |
pfam02927 | CelD_N | 3.66e-26 | 55 | 136 | 2 | 83 | Cellulase N-terminal ig-like domain. |
cd02850 | E_set_Cellulase_N | 1.54e-24 | 55 | 141 | 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. |
COG0726 | CDA1 | 6.71e-24 | 595 | 869 | 6 | 261 | Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT35459.1 | 0.0 | 51 | 867 | 20 | 836 |
QPH59586.1 | 0.0 | 51 | 867 | 20 | 836 |
QUT98069.1 | 0.0 | 51 | 867 | 20 | 836 |
QUT66756.1 | 0.0 | 51 | 867 | 20 | 836 |
QQA29127.1 | 0.0 | 51 | 867 | 20 | 836 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3X17_A | 4.79e-37 | 56 | 617 | 18 | 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 | 2.16e-30 | 64 | 642 | 2 | 553 | Crystalstructure of Zn-binding triple mutant of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4] |
5U0H_A | 5.05e-27 | 64 | 642 | 2 | 553 | Crystalstructure of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4] |
4CJ0_A | 2.81e-21 | 53 | 541 | 27 | 492 | ChainA, ENDOGLUCANASE D [Acetivibrio thermocellus],4CJ1_A Chain A, ENDOGLUCANASE D [Acetivibrio thermocellus] |
1CLC_A | 2.94e-21 | 53 | 541 | 41 | 506 | ChainA, ENDOGLUCANASE CELD; EC: 3.2.1.4 [Acetivibrio thermocellus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14090 | 4.30e-21 | 56 | 634 | 341 | 919 | 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 |
P0C2S4 | 1.54e-20 | 53 | 541 | 27 | 492 | Endoglucanase D (Fragment) OS=Acetivibrio thermocellus OX=1515 GN=celD PE=1 SV=1 |
A3DDN1 | 1.66e-20 | 53 | 541 | 51 | 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 |
Q05156 | 4.72e-20 | 56 | 626 | 185 | 746 | Cellulase 1 OS=Streptomyces reticuli OX=1926 GN=cel1 PE=1 SV=1 |
P23658 | 1.88e-19 | 56 | 622 | 4 | 545 | Cellodextrinase OS=Butyrivibrio fibrisolvens OX=831 GN=ced1 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.939734 | 0.058915 | 0.000575 | 0.000217 | 0.000173 | 0.000370 |
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