Species | CAG-177 sp000431775 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; CAG-177; CAG-177 sp000431775 | |||||||||||
CAZyme ID | MGYG000002001_01793 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Alpha-galactosidase A | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 9379; End: 10677 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 164 | 409 | 3.5e-62 | 0.9388646288209607 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 8.21e-102 | 9 | 338 | 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 | 1.83e-93 | 2 | 348 | 24 | 381 | alpha-galactosidase |
PLN03231 | PLN03231 | 3.27e-88 | 9 | 346 | 1 | 349 | putative alpha-galactosidase; Provisional |
PLN02808 | PLN02808 | 3.04e-43 | 5 | 429 | 28 | 381 | alpha-galactosidase |
PLN02692 | PLN02692 | 5.44e-38 | 5 | 429 | 52 | 406 | alpha-galactosidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AGC68671.1 | 2.42e-200 | 4 | 431 | 5 | 429 |
AGI39682.1 | 2.42e-200 | 4 | 431 | 5 | 429 |
ANW99008.1 | 6.91e-200 | 4 | 431 | 5 | 429 |
ANX01536.1 | 9.81e-200 | 4 | 431 | 5 | 429 |
BCJ96060.1 | 1.64e-195 | 1 | 431 | 1 | 428 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4NX0_A | 1.52e-172 | 2 | 431 | 18 | 440 | 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 | 2.48e-171 | 2 | 431 | 18 | 440 | 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 | 7.04e-150 | 1 | 394 | 4 | 391 | ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125] |
1UAS_A | 9.46e-35 | 5 | 429 | 5 | 357 | ChainA, alpha-galactosidase [Oryza sativa] |
3A5V_A | 5.82e-32 | 5 | 432 | 5 | 391 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8RX86 | 2.87e-37 | 1 | 431 | 32 | 391 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
P14749 | 1.39e-36 | 5 | 429 | 52 | 405 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q9FXT4 | 1.37e-33 | 5 | 429 | 60 | 412 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
Q42656 | 6.73e-33 | 5 | 429 | 20 | 373 | Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1 |
Q8VXZ7 | 4.53e-32 | 1 | 429 | 65 | 425 | Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000063 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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