Species | Eisenbergiella sp900555195 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900555195 | |||||||||||
CAZyme ID | MGYG000004136_02714 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1719; End: 3062 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 163 | 423 | 1.1e-61 | 0.9650655021834061 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 4.46e-107 | 10 | 341 | 1 | 267 | 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 | 3.73e-81 | 7 | 342 | 28 | 375 | alpha-galactosidase |
PLN03231 | PLN03231 | 2.35e-76 | 10 | 342 | 1 | 345 | putative alpha-galactosidase; Provisional |
PLN02808 | PLN02808 | 3.08e-50 | 4 | 447 | 26 | 383 | alpha-galactosidase |
PLN02692 | PLN02692 | 2.63e-44 | 4 | 447 | 50 | 408 | alpha-galactosidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QHQ63254.1 | 2.02e-232 | 1 | 447 | 1 | 436 |
QOV18098.1 | 1.26e-215 | 1 | 447 | 1 | 440 |
AEN96322.1 | 4.40e-215 | 11 | 447 | 37 | 463 |
QQQ91692.1 | 2.41e-212 | 1 | 445 | 1 | 432 |
ASU31152.1 | 2.41e-212 | 1 | 445 | 1 | 432 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4NX0_A | 3.54e-155 | 1 | 398 | 16 | 408 | 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 | 5.77e-154 | 1 | 398 | 16 | 408 | 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 | 2.22e-142 | 7 | 389 | 9 | 386 | ChainA, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125] |
6F4C_B | 2.38e-34 | 3 | 447 | 2 | 360 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
1UAS_A | 5.59e-32 | 3 | 447 | 2 | 359 | ChainA, alpha-galactosidase [Oryza sativa] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14749 | 1.44e-40 | 3 | 447 | 49 | 407 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q8RX86 | 7.67e-40 | 3 | 447 | 33 | 391 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
Q9FT97 | 5.06e-38 | 4 | 447 | 48 | 406 | Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 SV=1 |
Q42656 | 1.34e-35 | 4 | 447 | 18 | 375 | Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1 |
Q8VXZ7 | 2.23e-32 | 3 | 447 | 66 | 427 | 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 |
---|---|---|---|---|---|
1.000066 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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