Species | Sordaria macrospora | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Sordariaceae; Sordaria; Sordaria macrospora | |||||||||||
CAZyme ID | SMAC_11830-t26_1-p1 | |||||||||||
CAZy Family | GT62 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.88:1 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 10 | 92 | 2.4e-21 | 0.3537117903930131 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
269893 | GH27 | 7.34e-24 | 4 | 95 | 130 | 223 | 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. |
178487 | PLN02899 | 1.52e-14 | 11 | 93 | 226 | 316 | alpha-galactosidase |
178770 | PLN03231 | 5.96e-13 | 6 | 93 | 190 | 286 | putative alpha-galactosidase; Provisional |
374582 | Melibiase_2 | 1.67e-08 | 16 | 95 | 149 | 237 | Alpha galactosidase A. |
166449 | PLN02808 | 5.80e-08 | 16 | 91 | 170 | 244 | alpha-galactosidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
3.61e-50 | 1 | 95 | 216 | 310 | |
6.04e-50 | 1 | 95 | 222 | 316 | |
9.97e-50 | 1 | 95 | 181 | 275 | |
1.99e-49 | 1 | 95 | 196 | 290 | |
3.35e-49 | 1 | 95 | 191 | 285 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.59e-26 | 2 | 95 | 189 | 282 | Chain A, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125] |
|
1.33e-24 | 2 | 95 | 202 | 295 | Crystal structure 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] |
|
1.33e-24 | 2 | 95 | 202 | 295 | Crystal structure 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] |
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2.17e-07 | 18 | 95 | 159 | 245 | The Structure of alpha-N-Acetylgalactosaminidase [Gallus gallus],1KTC_A The Structure of alpha-N-Acetylgalactosaminidase [Gallus gallus] |
|
7.57e-07 | 16 | 95 | 157 | 244 | Chain A, Alpha-galactosidase A [Homo sapiens],3LX9_B Chain B, Alpha-galactosidase A [Homo sapiens],3LXA_A Chain A, Alpha-galactosidase A [Homo sapiens],3LXA_B Chain B, Alpha-galactosidase A [Homo sapiens],3LXB_A Chain A, Alpha-galactosidase A [Homo sapiens],3LXB_B Chain B, Alpha-galactosidase A [Homo sapiens],3LXC_A Chain A, Alpha-galactosidase A [Homo sapiens],3LXC_B Chain B, Alpha-galactosidase A [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.12e-06 | 16 | 95 | 173 | 261 | Alpha-N-acetylgalactosaminidase OS=Bos taurus OX=9913 GN=NAGA PE=2 SV=1 |
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1.12e-06 | 18 | 95 | 159 | 245 | Alpha-N-acetylgalactosaminidase OS=Gallus gallus OX=9031 GN=NAGA PE=1 SV=1 |
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2.98e-06 | 4 | 91 | 171 | 257 | Probable alpha-galactosidase D OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=aglD PE=3 SV=1 |
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5.34e-06 | 16 | 95 | 173 | 261 | Alpha-N-acetylgalactosaminidase OS=Mus musculus OX=10090 GN=Naga PE=1 SV=2 |
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9.97e-06 | 50 | 91 | 235 | 276 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000033 | 0.000028 |
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