| Species | UMGS1002 sp900547565 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS1002; UMGS1002 sp900547565 | |||||||||||
| CAZyme ID | MGYG000001934_01334 | |||||||||||
| CAZy Family | GH39 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 264; End: 1709 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH39 | 62 | 231 | 2.2e-29 | 0.382830626450116 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam01229 | Glyco_hydro_39 | 2.49e-11 | 64 | 239 | 70 | 239 | Glycosyl hydrolases family 39. |
| pfam02449 | Glyco_hydro_42 | 1.81e-05 | 27 | 80 | 4 | 56 | Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues. |
| cd21510 | agarase_cat | 8.72e-04 | 141 | 280 | 102 | 247 | alpha-beta barrel catalytic domain of agarase, such as GH86-like endo-acting agarases identified in non-marine organisms. Typically, agarases (E.C. 3.2.1.81) are found in ocean-dwelling bacteria since agarose is a principle component of red algae cell wall polysaccharides. Agarose is a linear polymer of alternating D-galactose and 3,6-anhydro-L-galactopyranose. Endo-acting agarases, such as glycoside hydrolase 16 (GH16) and GH86 hydrolyze internal beta-1,4 linkages. GH86-like endo-acting agarase of this protein family has been identified in the human intestinal bacterium Bacteroides uniformis. This acquired metabolic pathway, as demonstrated by the prevalence of agar-specific genetic cluster called polysaccharide utilization loci (PULs), varies considerably between human populations, being much more prevalent in a Japanese sample than in North America, European, or Chinese samples. Agarase activity was also identified in the non-marine bacterium Cellvibrio sp. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QYY35369.1 | 1.51e-150 | 1 | 479 | 1 | 473 |
| AWI10371.1 | 1.96e-142 | 3 | 479 | 60 | 528 |
| AVM45335.1 | 4.21e-139 | 1 | 479 | 10 | 477 |
| ASV73290.1 | 2.93e-68 | 7 | 477 | 70 | 524 |
| QNN22730.1 | 1.01e-64 | 3 | 360 | 46 | 375 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4EKJ_A | 7.75e-11 | 57 | 359 | 70 | 360 | ChainA, Beta-xylosidase [Caulobacter vibrioides] |
| 6UQJ_A | 7.87e-11 | 65 | 229 | 83 | 239 | Crystalstructure of the GH39 enzyme from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306] |
| 4M29_A | 1.03e-10 | 57 | 229 | 70 | 234 | Structureof a GH39 Beta-xylosidase from Caulobacter crescentus [Caulobacter vibrioides CB15] |
| 4ZN2_A | 4.23e-08 | 35 | 410 | 30 | 370 | Glycosylhydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_B Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_C Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_D Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1] |
| 5BX9_A | 4.23e-08 | 35 | 410 | 30 | 370 | Structureof PslG from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5BXA_A Structure of PslG from Pseudomonas aeruginosa in complex with mannose [Pseudomonas aeruginosa PAO1] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q9ZFM2 | 7.81e-06 | 65 | 197 | 74 | 200 | Beta-xylosidase OS=Geobacillus stearothermophilus OX=1422 GN=xynB PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000039 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.