Species | Prevotella sp002300055 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp002300055 | |||||||||||
CAZyme ID | MGYG000004632_01023 | |||||||||||
CAZy Family | GH20 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 198; End: 2384 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH20 | 350 | 698 | 8.3e-100 | 0.9554896142433235 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06563 | GH20_chitobiase-like | 1.30e-141 | 351 | 710 | 4 | 357 | 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 | 7.44e-114 | 351 | 697 | 4 | 345 | Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. |
cd06568 | GH20_SpHex_like | 3.21e-94 | 351 | 710 | 4 | 329 | 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. |
COG3525 | Chb | 7.76e-82 | 245 | 712 | 160 | 630 | N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]. |
cd06562 | GH20_HexA_HexB-like | 6.13e-67 | 351 | 721 | 4 | 348 | Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUB76505.1 | 7.87e-254 | 52 | 727 | 57 | 721 |
QUB65885.1 | 1.47e-251 | 52 | 727 | 57 | 721 |
QUB45992.1 | 8.37e-251 | 41 | 727 | 48 | 721 |
ANR73104.1 | 8.37e-251 | 41 | 727 | 48 | 721 |
QUB73127.1 | 6.77e-250 | 52 | 727 | 57 | 721 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6JE8_A | 1.25e-93 | 287 | 727 | 32 | 457 | crystalstructure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEA_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEB_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835] |
6Q63_A | 5.14e-79 | 219 | 713 | 31 | 525 | BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron] |
7CBN_A | 3.47e-67 | 293 | 724 | 78 | 510 | Crystalstructure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835],7CBO_A Crystal structure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila in complex with GlcNAc [Akkermansia muciniphila ATCC BAA-835] |
3RCN_A | 5.32e-66 | 274 | 710 | 62 | 498 | CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1] |
1HP4_A | 4.90e-64 | 292 | 724 | 97 | 503 | ChainA, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1HP5_A Chain A, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1JAK_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],1M01_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],5FCZ_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus],5FD0_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B2UP57 | 1.37e-92 | 287 | 727 | 53 | 478 | Beta-hexosaminidase Amuc_2018 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2018 PE=1 SV=1 |
P49008 | 4.83e-72 | 219 | 724 | 37 | 532 | Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2 |
B2UQG6 | 2.43e-66 | 293 | 724 | 97 | 529 | Beta-hexosaminidase Amuc_0868 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0868 PE=1 SV=1 |
P96155 | 1.14e-62 | 280 | 694 | 196 | 604 | Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1 |
Q7WUL4 | 3.56e-46 | 292 | 710 | 81 | 463 | Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.050074 | 0.937380 | 0.009652 | 0.002080 | 0.000442 | 0.000333 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.