Species | Barnesiella sp002159975 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp002159975 | |||||||||||
CAZyme ID | MGYG000001604_00773 | |||||||||||
CAZy Family | GH9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 146995; End: 149481 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH9 | 115 | 583 | 5.3e-78 | 0.992822966507177 |
CE4 | 610 | 743 | 9.4e-16 | 0.9307692307692308 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00759 | Glyco_hydro_9 | 1.72e-62 | 123 | 576 | 7 | 367 | Glycosyl hydrolase family 9. |
cd10917 | CE4_NodB_like_6s_7s | 1.78e-27 | 614 | 813 | 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. |
cd02850 | E_set_Cellulase_N | 1.95e-24 | 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. |
COG0726 | CDA1 | 2.41e-22 | 597 | 824 | 48 | 255 | Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
pfam02927 | CelD_N | 1.16e-20 | 24 | 103 | 2 | 81 | Cellulase N-terminal ig-like domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QPH59586.1 | 0.0 | 22 | 827 | 22 | 835 |
QUT35459.1 | 0.0 | 22 | 827 | 22 | 835 |
QUT98069.1 | 0.0 | 22 | 827 | 22 | 835 |
QUT66756.1 | 0.0 | 22 | 827 | 22 | 835 |
QQA29127.1 | 0.0 | 22 | 827 | 22 | 835 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3X17_A | 1.73e-37 | 22 | 582 | 15 | 552 | 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 | 1.01e-34 | 33 | 604 | 2 | 553 | Crystalstructure of Zn-binding triple mutant of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4] |
5U0H_A | 2.60e-31 | 33 | 604 | 2 | 553 | Crystalstructure of GH family 9 endoglucanase J30 [Thermobacillus composti KWC4] |
6DHT_A | 1.69e-23 | 17 | 586 | 10 | 564 | Bacteroidesovatus GH9 Bacova_02649 [Bacteroides ovatus ATCC 8483] |
4CJ0_A | 9.73e-20 | 25 | 510 | 30 | 492 | ChainA, ENDOGLUCANASE D [Acetivibrio thermocellus],4CJ1_A Chain A, ENDOGLUCANASE D [Acetivibrio thermocellus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14090 | 9.20e-30 | 22 | 591 | 338 | 912 | 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 | 7.81e-28 | 22 | 590 | 182 | 746 | Cellulase 1 OS=Streptomyces reticuli OX=1926 GN=cel1 PE=1 SV=1 |
A7LXT3 | 5.76e-23 | 12 | 586 | 19 | 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 |
P0C2S4 | 5.33e-19 | 25 | 510 | 30 | 492 | Endoglucanase D (Fragment) OS=Acetivibrio thermocellus OX=1515 GN=celD PE=1 SV=1 |
A3DDN1 | 5.67e-19 | 25 | 510 | 54 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000595 | 0.998639 | 0.000235 | 0.000177 | 0.000168 | 0.000167 |
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