Species | Bifidobacterium dentium | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium dentium | |||||||||||
CAZyme ID | MGYG000001354_00876 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1052836; End: 1054245 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 165 | 349 | 6.9e-47 | 0.7248908296943232 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 8.23e-93 | 14 | 341 | 1 | 268 | glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 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. GH27 members 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 have been identified as the catalytic nucleophile and the acid/base, respectively. |
PLN02899 | PLN02899 | 1.16e-88 | 11 | 351 | 28 | 385 | alpha-galactosidase |
PLN03231 | PLN03231 | 4.80e-75 | 14 | 351 | 1 | 355 | putative alpha-galactosidase; Provisional |
PLN02808 | PLN02808 | 9.35e-27 | 14 | 343 | 32 | 291 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 8.34e-23 | 14 | 335 | 2 | 275 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
VEG24632.1 | 0.0 | 1 | 469 | 1 | 469 |
BAQ29991.1 | 0.0 | 1 | 469 | 1 | 469 |
BAQ27962.1 | 0.0 | 1 | 469 | 1 | 469 |
QGM63451.1 | 0.0 | 1 | 469 | 1 | 469 |
QTL78851.1 | 0.0 | 16 | 469 | 1 | 454 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4NX0_A | 1.70e-119 | 14 | 365 | 25 | 377 | Crystalstructure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus] |
4NXK_A | 2.72e-118 | 14 | 365 | 25 | 377 | Crystalstructure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_B Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_C Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_D Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_E Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_F Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_G Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_H Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NZF_A Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_B Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_C Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_D Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_E Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_F Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_G Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_H Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus] |
3CC1_A | 5.08e-109 | 9 | 444 | 7 | 420 | ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125] |
3H53_A | 2.89e-24 | 14 | 407 | 9 | 352 | ChainA, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H53_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H54_A Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H54_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H55_A Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3H55_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],3IGU_A Chain A, Alpha-N-acetylgalactosaminidase [Homo sapiens],3IGU_B Chain B, Alpha-N-acetylgalactosaminidase [Homo sapiens],4DO4_A Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO4_B Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO5_A Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO5_B Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO6_A Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens],4DO6_B Pharmacological chaperones for human alpha-N-acetylgalactosaminidase [Homo sapiens] |
1UAS_A | 1.10e-21 | 14 | 345 | 9 | 273 | ChainA, alpha-galactosidase [Oryza sativa] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14749 | 3.36e-25 | 14 | 335 | 56 | 310 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q8RX86 | 3.80e-25 | 11 | 379 | 37 | 327 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
P17050 | 1.32e-23 | 14 | 407 | 26 | 369 | Alpha-N-acetylgalactosaminidase OS=Homo sapiens OX=9606 GN=NAGA PE=1 SV=2 |
B3PGJ1 | 1.16e-21 | 14 | 335 | 33 | 295 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
Q58DH9 | 4.12e-21 | 13 | 355 | 25 | 321 | Alpha-N-acetylgalactosaminidase OS=Bos taurus OX=9913 GN=NAGA PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000067 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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