Species | UMGS1633 sp900553645 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; UMGS1633; UMGS1633 sp900553645 | |||||||||||
CAZyme ID | MGYG000004044_00161 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Alpha-galactosidase A | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 33699; End: 34844 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 94 | 355 | 9.5e-60 | 0.9868995633187773 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 2.34e-131 | 1 | 272 | 3 | 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 | 7.88e-94 | 1 | 375 | 34 | 382 | alpha-galactosidase |
PLN02229 | PLN02229 | 1.02e-92 | 1 | 375 | 65 | 416 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 3.73e-85 | 1 | 272 | 4 | 284 | Alpha galactosidase A. |
PLN02692 | PLN02692 | 7.47e-83 | 1 | 377 | 58 | 409 | alpha-galactosidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QTE71472.1 | 2.05e-182 | 1 | 381 | 11 | 397 |
QTE75438.1 | 2.05e-182 | 1 | 381 | 11 | 397 |
QUC67774.1 | 4.13e-182 | 1 | 381 | 11 | 397 |
QUA53570.1 | 3.77e-180 | 1 | 381 | 10 | 396 |
QTE68632.1 | 1.43e-179 | 1 | 380 | 8 | 393 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1UAS_A | 5.07e-81 | 1 | 375 | 11 | 358 | ChainA, alpha-galactosidase [Oryza sativa] |
6F4C_B | 3.29e-79 | 1 | 375 | 11 | 359 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
4NZJ_A | 1.11e-77 | 2 | 276 | 103 | 390 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
4OGZ_A | 4.76e-75 | 2 | 272 | 103 | 386 | 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 | 2.02e-70 | 1 | 373 | 11 | 387 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14749 | 2.10e-83 | 1 | 375 | 58 | 406 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
B3PGJ1 | 5.40e-82 | 1 | 329 | 35 | 347 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
Q42656 | 8.90e-80 | 1 | 375 | 26 | 374 | Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1 |
Q9FXT4 | 1.38e-79 | 1 | 375 | 66 | 413 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
Q8RX86 | 2.37e-78 | 1 | 381 | 42 | 396 | 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 |
---|---|---|---|---|---|
1.000055 | 0.000000 | 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.