| Species | OM05-12 sp900760755 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OM05-12; OM05-12 sp900760755 | |||||||||||
| CAZyme ID | MGYG000003221_01952 | |||||||||||
| CAZy Family | GH20 | |||||||||||
| CAZyme Description | N,N'-diacetylchitobiase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 32378; End: 34891 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH20 | 315 | 726 | 6.4e-95 | 0.9525222551928784 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd06569 | GH20_Sm-chitobiase-like | 0.0 | 310 | 746 | 1 | 436 | 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 | 6.47e-105 | 315 | 725 | 2 | 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 | 5.95e-103 | 315 | 725 | 2 | 343 | Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. |
| COG3525 | Chb | 1.46e-97 | 51 | 811 | 25 | 689 | N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]. |
| cd06568 | GH20_SpHex_like | 1.60e-60 | 315 | 730 | 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 |
|---|---|---|---|---|---|
| QUT73869.1 | 0.0 | 1 | 837 | 1 | 837 |
| QUR46113.1 | 0.0 | 6 | 836 | 8 | 840 |
| QDH52947.1 | 0.0 | 6 | 836 | 8 | 840 |
| QRN00147.1 | 0.0 | 6 | 836 | 8 | 840 |
| CBK66887.1 | 0.0 | 14 | 836 | 7 | 831 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1QBA_A | 1.04e-87 | 263 | 820 | 262 | 844 | BACTERIALCHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20 [Serratia marcescens],1QBB_A BACTERIAL CHITOBIASE COMPLEXED WITH CHITOBIOSE (DINAG) [Serratia marcescens] |
| 1C7T_A | 1.99e-87 | 263 | 820 | 262 | 844 | ChainA, BETA-N-ACETYLHEXOSAMINIDASE [Serratia marcescens] |
| 1C7S_A | 1.01e-86 | 263 | 820 | 262 | 844 | ChainA, BETA-N-ACETYLHEXOSAMINIDASE [Serratia marcescens] |
| 6EZR_A | 3.57e-69 | 234 | 767 | 188 | 638 | 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 | 4.38e-68 | 234 | 767 | 185 | 635 | 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 |
|---|---|---|---|---|---|---|
| Q04786 | 1.35e-93 | 42 | 797 | 40 | 809 | Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1 |
| P13670 | 5.09e-91 | 42 | 797 | 64 | 846 | N,N'-diacetylchitobiase OS=Vibrio harveyi OX=669 GN=chb PE=1 SV=1 |
| Q54468 | 1.28e-86 | 263 | 820 | 289 | 871 | Chitobiase OS=Serratia marcescens OX=615 GN=chb PE=1 SV=1 |
| P49007 | 2.07e-86 | 42 | 726 | 53 | 727 | Beta-hexosaminidase B OS=Pseudoalteromonas piscicida OX=43662 GN=nag096 PE=3 SV=1 |
| P96155 | 7.62e-62 | 185 | 720 | 135 | 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 |
|---|---|---|---|---|---|
| 0.000008 | 0.006454 | 0.993578 | 0.000002 | 0.000003 | 0.000003 |
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