| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; | |||||||||||
| CAZyme ID | MGYG000001242_01183 | |||||||||||
| CAZy Family | GH20 | |||||||||||
| CAZyme Description | N,N'-diacetylchitobiase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 22; End: 1623 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH20 | 40 | 427 | 3.5e-79 | 0.9703264094955489 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd06569 | GH20_Sm-chitobiase-like | 4.11e-148 | 41 | 430 | 1 | 419 | 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 | 1.80e-86 | 45 | 426 | 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 | 2.57e-85 | 45 | 426 | 1 | 343 | Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. |
| COG3525 | Chb | 8.42e-76 | 33 | 530 | 249 | 715 | N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]. |
| cd06568 | GH20_SpHex_like | 1.10e-49 | 45 | 426 | 1 | 314 | 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 | 2.25e-175 | 10 | 531 | 234 | 748 |
| VTZ55501.1 | 9.50e-141 | 36 | 528 | 287 | 816 |
| QUT34090.1 | 1.42e-140 | 36 | 528 | 302 | 831 |
| BBK89309.1 | 3.75e-140 | 36 | 528 | 287 | 816 |
| QUU00208.1 | 5.59e-140 | 36 | 528 | 302 | 831 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1QBA_A | 1.37e-66 | 40 | 492 | 306 | 823 | BACTERIALCHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20 [Serratia marcescens],1QBB_A BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG) [Serratia marcescens] |
| 1C7T_A | 3.41e-65 | 40 | 492 | 306 | 823 | ChainA, BETA-N-ACETYLHEXOSAMINIDASE [Serratia marcescens] |
| 1C7S_A | 2.33e-64 | 40 | 492 | 306 | 823 | ChainA, BETA-N-ACETYLHEXOSAMINIDASE [Serratia marcescens] |
| 6EZR_A | 1.64e-61 | 39 | 426 | 257 | 608 | 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 | 2.13e-60 | 39 | 426 | 254 | 605 | 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] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P13670 | 4.00e-67 | 27 | 490 | 311 | 846 | N,N'-diacetylchitobiase OS=Vibrio harveyi OX=669 GN=chb PE=1 SV=1 |
| Q54468 | 1.40e-65 | 40 | 492 | 333 | 850 | Chitobiase OS=Serratia marcescens OX=615 GN=chb PE=1 SV=1 |
| Q04786 | 1.13e-63 | 39 | 490 | 309 | 809 | Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1 |
| P49007 | 1.23e-57 | 26 | 427 | 309 | 727 | Beta-hexosaminidase B OS=Pseudoalteromonas piscicida OX=43662 GN=nag096 PE=3 SV=1 |
| P96155 | 5.51e-54 | 30 | 425 | 245 | 604 | Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000049 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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