Species | Eisenbergiella sp900539715 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900539715 | |||||||||||
CAZyme ID | MGYG000000312_00069 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Alpha-galactosidase A | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 71310; End: 72440 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 100 | 349 | 3.7e-75 | 0.9868995633187773 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 8.07e-146 | 6 | 278 | 1 | 271 | 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. |
PLN02808 | PLN02808 | 3.16e-110 | 4 | 369 | 30 | 381 | alpha-galactosidase |
PLN02229 | PLN02229 | 7.25e-110 | 4 | 369 | 61 | 415 | alpha-galactosidase |
PLN02692 | PLN02692 | 1.20e-100 | 4 | 375 | 54 | 412 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 5.94e-97 | 5 | 278 | 1 | 284 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
VCV24057.1 | 1.24e-230 | 1 | 376 | 1 | 376 |
QAA34453.1 | 8.82e-165 | 1 | 375 | 1 | 374 |
QUL57156.1 | 4.32e-162 | 4 | 374 | 14 | 392 |
AIQ57865.1 | 7.30e-162 | 4 | 374 | 9 | 387 |
AIQ29066.1 | 1.47e-161 | 4 | 374 | 9 | 387 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1UAS_A | 4.50e-95 | 5 | 369 | 8 | 357 | ChainA, alpha-galactosidase [Oryza sativa] |
4NZJ_A | 6.25e-92 | 4 | 369 | 98 | 471 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
6F4C_B | 2.75e-88 | 5 | 369 | 8 | 358 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
4OGZ_A | 3.43e-87 | 4 | 326 | 98 | 431 | Crystalstructure of a putative alpha-galactosidase/melibiase (BF4189) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343],4OGZ_B Crystal structure of a putative alpha-galactosidase/melibiase (BF4189) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343] |
3A5V_A | 6.07e-81 | 2 | 345 | 5 | 364 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14749 | 2.67e-100 | 5 | 369 | 55 | 405 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q8VXZ7 | 1.08e-94 | 5 | 369 | 72 | 425 | Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1 |
Q9FXT4 | 1.33e-93 | 5 | 369 | 63 | 412 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
B3PGJ1 | 5.09e-93 | 5 | 320 | 32 | 343 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
Q8RX86 | 2.25e-92 | 2 | 369 | 36 | 389 | 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 |
---|---|---|---|---|---|
1.000057 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.