| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; SFTJ01; | |||||||||||
| CAZyme ID | MGYG000002176_01559 | |||||||||||
| CAZy Family | GH20 | |||||||||||
| CAZyme Description | N,N'-diacetylchitobiase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 5016; End: 7514 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH20 | 303 | 719 | 3.6e-84 | 0.973293768545994 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd06569 | GH20_Sm-chitobiase-like | 5.69e-155 | 304 | 725 | 1 | 423 | 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. |
| pfam00728 | Glyco_hydro_20 | 6.90e-83 | 308 | 719 | 1 | 345 | Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. |
| cd06563 | GH20_chitobiase-like | 8.69e-81 | 308 | 723 | 1 | 350 | 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. |
| COG3525 | Chb | 7.21e-75 | 45 | 795 | 21 | 704 | N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]. |
| cd06568 | GH20_SpHex_like | 1.24e-51 | 308 | 725 | 1 | 324 | 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 |
|---|---|---|---|---|---|
| AHF12728.1 | 1.36e-212 | 24 | 827 | 26 | 829 |
| QPH57903.1 | 5.63e-187 | 24 | 832 | 29 | 834 |
| QMI79073.1 | 8.85e-186 | 24 | 832 | 29 | 834 |
| BBK89309.1 | 1.12e-185 | 24 | 832 | 14 | 819 |
| QBJ17558.1 | 1.76e-185 | 24 | 832 | 29 | 834 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1QBA_A | 4.40e-73 | 187 | 792 | 190 | 823 | BACTERIALCHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20 [Serratia marcescens],1QBB_A BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG) [Serratia marcescens] |
| 1C7T_A | 8.29e-73 | 187 | 792 | 190 | 823 | ChainA, BETA-N-ACETYLHEXOSAMINIDASE [Serratia marcescens] |
| 1C7S_A | 4.04e-72 | 187 | 792 | 190 | 823 | ChainA, BETA-N-ACETYLHEXOSAMINIDASE [Serratia marcescens] |
| 6EZR_A | 3.55e-58 | 220 | 723 | 173 | 616 | 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 | 4.12e-57 | 220 | 723 | 170 | 613 | 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 | 2.49e-76 | 44 | 790 | 68 | 846 | N,N'-diacetylchitobiase OS=Vibrio harveyi OX=669 GN=chb PE=1 SV=1 |
| Q04786 | 6.62e-75 | 23 | 790 | 29 | 809 | Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1 |
| Q54468 | 6.64e-72 | 187 | 792 | 217 | 850 | Chitobiase OS=Serratia marcescens OX=615 GN=chb PE=1 SV=1 |
| P49007 | 1.04e-70 | 133 | 718 | 161 | 727 | Beta-hexosaminidase B OS=Pseudoalteromonas piscicida OX=43662 GN=nag096 PE=3 SV=1 |
| P96155 | 8.60e-57 | 244 | 712 | 197 | 600 | 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 |
|---|---|---|---|---|---|
| 0.000249 | 0.999122 | 0.000158 | 0.000169 | 0.000148 | 0.000143 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.