Species | Leclercia adecarboxylata_C | |||||||||||
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Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Leclercia; Leclercia adecarboxylata_C | |||||||||||
CAZyme ID | MGYG000003187_01075 | |||||||||||
CAZy Family | GH20 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 88984; End: 91368 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH20 | 154 | 585 | 4e-120 | 0.9762611275964391 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06570 | GH20_chitobiase-like_1 | 3.28e-173 | 159 | 597 | 1 | 311 | 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. |
cd06563 | GH20_chitobiase-like | 4.08e-132 | 159 | 597 | 1 | 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 | 8.45e-120 | 159 | 584 | 1 | 345 | Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. |
cd06562 | GH20_HexA_HexB-like | 2.33e-107 | 159 | 600 | 1 | 340 | 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. |
COG3525 | Chb | 1.04e-82 | 27 | 409 | 136 | 539 | N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QGU13607.1 | 0.0 | 1 | 794 | 1 | 794 |
QDK19036.1 | 0.0 | 1 | 794 | 1 | 794 |
QFH63607.1 | 0.0 | 1 | 794 | 1 | 794 |
QGP82150.1 | 0.0 | 1 | 794 | 1 | 794 |
QIG27178.1 | 0.0 | 1 | 794 | 1 | 794 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6YHH_A | 1.95e-120 | 24 | 762 | 6 | 648 | X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101] |
7CBN_A | 3.02e-72 | 107 | 384 | 78 | 377 | 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 | 7.24e-67 | 73 | 418 | 78 | 442 | BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron] |
1NOU_A | 1.44e-60 | 89 | 597 | 80 | 480 | Nativehuman lysosomal beta-hexosaminidase isoform B [Homo sapiens],1NOU_B Native human lysosomal beta-hexosaminidase isoform B [Homo sapiens],1NOW_A Human lysosomal beta-hexosaminidase isoform B in complex with (2R,3R,4S,5R)-2-Acetamido-3,4-Dihydroxy-5-Hydroxymethyl-Piperidinium Chloride (GalNAc-isofagomine) [Homo sapiens],1NOW_B Human lysosomal beta-hexosaminidase isoform B in complex with (2R,3R,4S,5R)-2-Acetamido-3,4-Dihydroxy-5-Hydroxymethyl-Piperidinium Chloride (GalNAc-isofagomine) [Homo sapiens],2GJX_B Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_C Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_F Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_G Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens] |
1O7A_A | 1.72e-60 | 89 | 597 | 88 | 488 | Humanbeta-Hexosaminidase B [Homo sapiens],1O7A_B Human beta-Hexosaminidase B [Homo sapiens],1O7A_C Human beta-Hexosaminidase B [Homo sapiens],1O7A_D Human beta-Hexosaminidase B [Homo sapiens],1O7A_E Human beta-Hexosaminidase B [Homo sapiens],1O7A_F Human beta-Hexosaminidase B [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P49008 | 5.66e-77 | 31 | 409 | 39 | 432 | Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2 |
B2UQG6 | 2.15e-71 | 107 | 384 | 97 | 396 | 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 | 1.47e-66 | 19 | 409 | 133 | 532 | Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1 |
P20060 | 9.08e-63 | 85 | 597 | 104 | 508 | Beta-hexosaminidase subunit beta OS=Mus musculus OX=10090 GN=Hexb PE=1 SV=2 |
P49614 | 7.77e-62 | 101 | 597 | 115 | 503 | Beta-hexosaminidase subunit beta OS=Felis catus OX=9685 GN=HEXB PE=2 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000353 | 0.998856 | 0.000187 | 0.000216 | 0.000202 | 0.000170 |
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