Species | Lentilactobacillus parafarraginis | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lentilactobacillus; Lentilactobacillus parafarraginis | |||||||||||
CAZyme ID | MGYG000002542_02228 | |||||||||||
CAZy Family | GH20 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 4170; End: 5306 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH20 | 38 | 353 | 4e-44 | 0.8813056379821959 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06564 | GH20_DspB_LnbB-like | 2.54e-45 | 38 | 363 | 3 | 311 | Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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. |
cd02742 | GH20_hexosaminidase | 7.01e-40 | 39 | 360 | 3 | 286 | Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) 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. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself. |
pfam00728 | Glyco_hydro_20 | 1.13e-19 | 39 | 349 | 5 | 318 | Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. |
COG3525 | Chb | 1.20e-19 | 39 | 270 | 265 | 521 | N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]. |
cd06563 | GH20_chitobiase-like | 3.02e-19 | 39 | 204 | 5 | 175 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AMV63908.1 | 4.65e-263 | 21 | 378 | 1 | 358 |
AMV68250.1 | 4.65e-263 | 21 | 378 | 1 | 358 |
QIR10640.1 | 1.12e-192 | 3 | 378 | 2 | 377 |
QEU39826.1 | 6.19e-188 | 10 | 378 | 1 | 369 |
QHB53470.1 | 1.25e-187 | 10 | 378 | 1 | 369 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1YHT_A | 1.70e-54 | 39 | 369 | 20 | 351 | Crystalstructure analysis of Dispersin B [Aggregatibacter actinomycetemcomitans] |
3RCN_A | 6.25e-12 | 36 | 204 | 139 | 316 | CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1] |
6Q63_A | 3.17e-11 | 36 | 258 | 160 | 389 | BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron] |
6EZR_A | 3.89e-11 | 37 | 232 | 265 | 460 | 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 | 3.79e-10 | 37 | 232 | 262 | 457 | 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 |
---|---|---|---|---|---|---|
Q54468 | 7.29e-09 | 37 | 204 | 340 | 540 | Chitobiase OS=Serratia marcescens OX=615 GN=chb PE=1 SV=1 |
Q7WUL4 | 1.26e-07 | 37 | 262 | 137 | 350 | Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1 |
P20060 | 4.09e-07 | 39 | 204 | 183 | 334 | Beta-hexosaminidase subunit beta OS=Mus musculus OX=10090 GN=Hexb PE=1 SV=2 |
P49610 | 1.26e-06 | 28 | 297 | 175 | 470 | Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2 |
P49007 | 2.59e-06 | 25 | 288 | 317 | 619 | Beta-hexosaminidase B OS=Pseudoalteromonas piscicida OX=43662 GN=nag096 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000356 | 0.275981 | 0.723240 | 0.000145 | 0.000138 | 0.000124 |
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