Species | UMGS1826 sp900555435 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UMGS1826; UMGS1826 sp900555435 | |||||||||||
CAZyme ID | MGYG000000537_01262 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Alpha-galactosidase A | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 11874; End: 13007 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 101 | 350 | 2.4e-65 | 0.9868995633187773 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 2.42e-142 | 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 | 2.91e-109 | 2 | 369 | 28 | 381 | alpha-galactosidase |
PLN02229 | PLN02229 | 2.60e-97 | 2 | 369 | 59 | 415 | alpha-galactosidase |
PLN02692 | PLN02692 | 4.40e-97 | 2 | 372 | 52 | 409 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 6.41e-97 | 6 | 278 | 2 | 284 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QTE68632.1 | 3.90e-183 | 1 | 375 | 1 | 393 |
QTE71472.1 | 2.04e-181 | 1 | 374 | 4 | 395 |
QTE75438.1 | 2.04e-181 | 1 | 374 | 4 | 395 |
QUC67774.1 | 2.04e-181 | 1 | 374 | 4 | 395 |
QUA53570.1 | 6.52e-180 | 1 | 374 | 3 | 394 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6F4C_B | 2.23e-90 | 2 | 369 | 5 | 358 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
1UAS_A | 9.76e-89 | 2 | 369 | 5 | 357 | ChainA, alpha-galactosidase [Oryza sativa] |
4OGZ_A | 9.66e-84 | 2 | 278 | 96 | 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] |
4NZJ_A | 1.03e-80 | 2 | 278 | 96 | 386 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
3A5V_A | 7.80e-79 | 2 | 370 | 5 | 389 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14749 | 3.20e-96 | 2 | 369 | 52 | 405 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q8RX86 | 1.86e-91 | 2 | 369 | 36 | 389 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
B3PGJ1 | 2.69e-87 | 2 | 326 | 29 | 351 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
Q9FXT4 | 2.79e-87 | 2 | 369 | 60 | 412 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
Q42656 | 3.12e-85 | 2 | 369 | 20 | 373 | Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.997303 | 0.002708 | 0.000015 | 0.000010 | 0.000004 | 0.000009 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.