Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; | |||||||||||
CAZyme ID | MGYG000004430_00673 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 24610; End: 27450 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 189 | 398 | 3e-57 | 0.8558951965065502 |
CBM51 | 467 | 626 | 1.4e-26 | 0.9776119402985075 |
CBM51 | 635 | 721 | 2.9e-17 | 0.5970149253731343 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 3.88e-99 | 34 | 356 | 1 | 266 | 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 | 4.39e-88 | 28 | 367 | 25 | 384 | alpha-galactosidase |
PLN03231 | PLN03231 | 8.43e-83 | 34 | 368 | 1 | 355 | putative alpha-galactosidase; Provisional |
pfam16499 | Melibiase_2 | 2.34e-36 | 33 | 356 | 1 | 279 | Alpha galactosidase A. |
PLN02808 | PLN02808 | 9.23e-33 | 29 | 407 | 27 | 340 | alpha-galactosidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
APU68995.1 | 4.41e-231 | 24 | 552 | 33 | 560 |
QIL77713.1 | 1.04e-212 | 24 | 551 | 26 | 550 |
QDA61431.1 | 1.04e-210 | 5 | 551 | 11 | 552 |
QNE38644.1 | 1.79e-207 | 25 | 551 | 29 | 552 |
QNP52204.1 | 1.22e-205 | 1 | 517 | 1 | 517 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4NX0_A | 1.73e-142 | 30 | 393 | 21 | 387 | 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 | 2.68e-141 | 30 | 393 | 21 | 387 | 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 | 3.29e-129 | 31 | 393 | 9 | 374 | ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125] |
1UAS_A | 6.11e-28 | 29 | 409 | 4 | 319 | ChainA, alpha-galactosidase [Oryza sativa] |
1KTB_A | 2.73e-24 | 29 | 375 | 4 | 308 | TheStructure of alpha-N-Acetylgalactosaminidase [Gallus gallus],1KTC_A The Structure of alpha-N-Acetylgalactosaminidase [Gallus gallus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14749 | 9.85e-31 | 29 | 417 | 51 | 374 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
B3PGJ1 | 6.20e-28 | 18 | 364 | 18 | 307 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
Q9FXT4 | 8.12e-27 | 29 | 409 | 59 | 374 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
Q8VXZ7 | 1.44e-26 | 29 | 393 | 68 | 371 | Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1 |
Q8RX86 | 1.44e-26 | 29 | 364 | 35 | 306 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000238 | 0.999106 | 0.000146 | 0.000170 | 0.000152 | 0.000142 |
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