Species | Levilactobacillus brevis | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Levilactobacillus; Levilactobacillus brevis | |||||||||||
CAZyme ID | MGYG000002380_01231 | |||||||||||
CAZy Family | GH31 | |||||||||||
CAZyme Description | Alpha-xylosidase XylQ | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 36885; End: 37697 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK10658 | PRK10658 | 5.00e-164 | 1 | 270 | 1 | 271 | putative alpha-glucosidase; Provisional |
COG1501 | YicI | 1.15e-45 | 8 | 268 | 1 | 267 | Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism]. |
cd14752 | GH31_N | 3.76e-35 | 148 | 257 | 10 | 122 | N-terminal domain of glycosyl hydrolase family 31 (GH31). This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite-1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket. |
pfam13802 | Gal_mutarotas_2 | 3.97e-13 | 157 | 217 | 1 | 67 | Galactose mutarotase-like. This family is found N-terminal to glycosyl-hydrolase domains, and appears to be similar to the galactose mutarotase superfamily. |
pfam01055 | Glyco_hydro_31 | 3.49e-11 | 238 | 270 | 1 | 33 | Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AWP45919.1 | 2.51e-196 | 1 | 270 | 1 | 270 |
ARN90722.1 | 2.51e-196 | 1 | 270 | 1 | 270 |
ARN98350.1 | 2.51e-196 | 1 | 270 | 1 | 270 |
ARW21378.1 | 3.56e-196 | 1 | 270 | 1 | 270 |
QOP51924.1 | 3.56e-196 | 1 | 270 | 1 | 270 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2F2H_A | 5.08e-77 | 1 | 270 | 1 | 272 | Structureof the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_B Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_C Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_D Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_E Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_F Structure of the YicI thiosugar Michaelis complex [Escherichia coli] |
1XSI_A | 5.51e-77 | 1 | 270 | 1 | 272 | Structureof a Family 31 alpha glycosidase [Escherichia coli],1XSI_B Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_C Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_D Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_E Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_F Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_A Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_B Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_C Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_D Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_E Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_F Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSK_A Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_B Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_C Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_D Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_E Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_F Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli] |
1WE5_A | 1.47e-74 | 2 | 270 | 2 | 272 | CrystalStructure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_B Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_C Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_D Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_E Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli],1WE5_F Crystal Structure of Alpha-Xylosidase from Escherichia coli [Escherichia coli] |
5F7C_A | 4.78e-19 | 157 | 270 | 201 | 315 | Crystalstructure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_B Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_C Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5F7C_D Crystal structure of Family 31 alpha-glucosidase (BT_0339) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
6JR8_A | 1.65e-18 | 129 | 268 | 121 | 269 | Flavobacteriumjohnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101],6JR8_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A, mutant D412A complexed with isomaltotriose [Flavobacterium johnsoniae UW101] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P96793 | 5.76e-117 | 1 | 270 | 1 | 270 | Alpha-xylosidase XylQ OS=Lactiplantibacillus pentosus OX=1589 GN=xylQ PE=1 SV=1 |
P31434 | 2.74e-76 | 1 | 270 | 1 | 272 | Alpha-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yicI PE=1 SV=2 |
Q5AW25 | 2.73e-58 | 1 | 270 | 1 | 290 | Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD PE=1 SV=1 |
Q9F234 | 3.98e-17 | 89 | 268 | 83 | 263 | Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1 |
P0CD66 | 2.64e-11 | 144 | 268 | 50 | 178 | Alpha-glucosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=malA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000048 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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