Species | Alistipes_A sp900546005 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900546005 | |||||||||||
CAZyme ID | MGYG000004105_00389 | |||||||||||
CAZy Family | GH20 | |||||||||||
CAZyme Description | Beta-hexosaminidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 53914; End: 55515 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH20 | 150 | 500 | 7.5e-110 | 0.9762611275964391 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06563 | GH20_chitobiase-like | 5.43e-165 | 156 | 512 | 1 | 356 | 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 | 1.83e-131 | 156 | 500 | 1 | 345 | Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. |
COG3525 | Chb | 3.45e-99 | 17 | 513 | 125 | 628 | N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]. |
cd06570 | GH20_chitobiase-like_1 | 2.81e-93 | 156 | 512 | 1 | 310 | A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase 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 subgroup 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. |
cd06562 | GH20_HexA_HexB-like | 3.29e-80 | 156 | 513 | 1 | 337 | 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 |
---|---|---|---|---|---|
QGA24333.1 | 0.0 | 1 | 533 | 1 | 532 |
SCM59072.1 | 9.85e-237 | 1 | 529 | 1 | 526 |
CAZ97490.1 | 4.38e-159 | 9 | 524 | 8 | 526 |
BCI64811.1 | 1.94e-156 | 26 | 524 | 21 | 518 |
ALJ60896.1 | 1.54e-152 | 1 | 524 | 1 | 525 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7CBN_A | 2.19e-89 | 124 | 512 | 98 | 495 | 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] |
6Q63_A | 7.95e-84 | 17 | 525 | 21 | 534 | BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron] |
7DUP_A | 3.38e-82 | 26 | 525 | 4 | 518 | ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron] |
7DVB_A | 1.84e-81 | 26 | 525 | 4 | 518 | ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_C Chain C, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_D Chain D, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron] |
6YHH_A | 2.38e-80 | 95 | 524 | 88 | 502 | X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B2UQG6 | 1.60e-88 | 124 | 512 | 117 | 514 | 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 | 6.14e-81 | 25 | 497 | 138 | 604 | Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1 |
P49008 | 7.09e-79 | 23 | 512 | 32 | 517 | Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2 |
B2UP57 | 1.59e-57 | 91 | 512 | 51 | 461 | 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 |
Q8L7S6 | 4.52e-47 | 85 | 503 | 108 | 489 | Beta-hexosaminidase 3 OS=Arabidopsis thaliana OX=3702 GN=HEXO3 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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0.000295 | 0.998950 | 0.000278 | 0.000172 | 0.000160 | 0.000137 |
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