Species | Prevotella sp900290275 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900290275 | |||||||||||
CAZyme ID | MGYG000002108_00606 | |||||||||||
CAZy Family | GH20 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 15223; End: 17412 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH20 | 352 | 699 | 3.9e-98 | 0.9525222551928784 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06563 | GH20_chitobiase-like | 8.25e-138 | 353 | 711 | 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 | 9.77e-114 | 353 | 699 | 4 | 345 | Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. |
cd06568 | GH20_SpHex_like | 4.90e-91 | 353 | 711 | 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 | 4.80e-78 | 290 | 712 | 201 | 629 | N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]. |
cd06562 | GH20_HexA_HexB-like | 1.20e-64 | 353 | 722 | 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 | 5.91e-241 | 52 | 723 | 57 | 716 |
QUB73127.1 | 1.19e-240 | 52 | 723 | 57 | 716 |
QUB40309.1 | 2.24e-238 | 52 | 723 | 62 | 737 |
BBA28593.1 | 2.51e-237 | 34 | 723 | 41 | 716 |
QUB65885.1 | 4.07e-236 | 52 | 723 | 57 | 716 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6JE8_A | 3.24e-89 | 281 | 721 | 23 | 451 | 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 | 7.28e-79 | 283 | 726 | 94 | 537 | BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron] |
3RCN_A | 2.65e-63 | 276 | 711 | 62 | 498 | CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1] |
1HP4_A | 1.80e-62 | 294 | 725 | 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] |
1M04_A | 9.15e-62 | 294 | 725 | 97 | 503 | ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B2UP57 | 3.50e-88 | 281 | 721 | 44 | 472 | 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 | 1.19e-69 | 280 | 725 | 95 | 532 | Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2 |
P96155 | 6.09e-63 | 216 | 703 | 138 | 611 | Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1 |
B2UQG6 | 2.71e-58 | 283 | 725 | 86 | 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 |
Q7WUL4 | 1.85e-43 | 294 | 722 | 81 | 474 | 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 |
---|---|---|---|---|---|
0.001299 | 0.997750 | 0.000265 | 0.000232 | 0.000222 | 0.000207 |
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