| Species | CAG-873 sp004552485 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp004552485 | |||||||||||
| CAZyme ID | MGYG000000673_00485 | |||||||||||
| CAZy Family | GH20 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 25660; End: 27882 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH20 | 253 | 637 | 4.2e-86 | 0.9673590504451038 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd06569 | GH20_Sm-chitobiase-like | 6.61e-137 | 252 | 653 | 1 | 433 | The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. |
| cd06563 | GH20_chitobiase-like | 1.88e-100 | 256 | 635 | 1 | 342 | The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. |
| pfam00728 | Glyco_hydro_20 | 8.65e-98 | 256 | 637 | 1 | 345 | Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. |
| COG3525 | Chb | 5.53e-82 | 245 | 712 | 250 | 689 | N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]. |
| cd06568 | GH20_SpHex_like | 1.13e-51 | 257 | 640 | 2 | 319 | A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QIM10820.1 | 4.58e-202 | 12 | 736 | 9 | 745 |
| AHF12728.1 | 1.65e-136 | 75 | 734 | 84 | 829 |
| VTZ55501.1 | 5.26e-133 | 241 | 739 | 277 | 819 |
| BBK89309.1 | 2.89e-132 | 241 | 739 | 277 | 819 |
| QMI79073.1 | 4.26e-132 | 241 | 739 | 292 | 834 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6EZR_A | 6.58e-67 | 235 | 643 | 239 | 618 | Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZR_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZS_A Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6EZS_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6K35_A Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi],6K35_B Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi] |
| 6EZT_A | 8.25e-66 | 235 | 643 | 236 | 615 | Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi],6EZT_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi] |
| 1QBA_A | 1.51e-55 | 225 | 698 | 278 | 821 | BACTERIALCHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20 [Serratia marcescens],1QBB_A BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG) [Serratia marcescens] |
| 1C7T_A | 2.78e-55 | 225 | 698 | 278 | 821 | ChainA, BETA-N-ACETYLHEXOSAMINIDASE [Serratia marcescens] |
| 1C7S_A | 1.28e-54 | 225 | 698 | 278 | 821 | ChainA, BETA-N-ACETYLHEXOSAMINIDASE [Serratia marcescens] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q04786 | 7.63e-65 | 171 | 698 | 228 | 809 | Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1 |
| P96155 | 7.59e-64 | 245 | 631 | 249 | 601 | Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1 |
| P13670 | 1.04e-63 | 208 | 698 | 284 | 846 | N,N'-diacetylchitobiase OS=Vibrio harveyi OX=669 GN=chb PE=1 SV=1 |
| P49007 | 5.17e-61 | 203 | 636 | 276 | 727 | Beta-hexosaminidase B OS=Pseudoalteromonas piscicida OX=43662 GN=nag096 PE=3 SV=1 |
| Q54468 | 7.57e-55 | 225 | 698 | 305 | 848 | Chitobiase OS=Serratia marcescens OX=615 GN=chb PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000374 | 0.998749 | 0.000193 | 0.000244 | 0.000211 | 0.000186 |
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