Species | Prevotellamassilia timonensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia; Prevotellamassilia timonensis | |||||||||||
CAZyme ID | MGYG000002412_02864 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Alpha-galactosidase A | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 1161598; End: 1162812 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 129 | 381 | 9.2e-77 | 0.9737991266375546 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 5.54e-136 | 33 | 317 | 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 | 2.74e-106 | 32 | 396 | 31 | 376 | alpha-galactosidase |
PLN02229 | PLN02229 | 1.88e-100 | 29 | 386 | 59 | 399 | alpha-galactosidase |
PLN02692 | PLN02692 | 3.19e-100 | 29 | 382 | 52 | 386 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 2.83e-90 | 32 | 317 | 1 | 284 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BBA29384.1 | 1.12e-185 | 8 | 403 | 11 | 406 |
QUB45459.1 | 1.30e-184 | 9 | 403 | 13 | 406 |
ANR72335.1 | 1.30e-184 | 9 | 403 | 13 | 406 |
QUB68250.1 | 1.50e-183 | 8 | 403 | 11 | 406 |
QUB83898.1 | 2.13e-183 | 23 | 404 | 27 | 407 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4NZJ_A | 6.40e-106 | 13 | 358 | 80 | 427 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
4OGZ_A | 9.04e-105 | 28 | 402 | 95 | 471 | 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] |
1UAS_A | 2.91e-92 | 32 | 403 | 8 | 359 | ChainA, alpha-galactosidase [Oryza sativa] |
6F4C_B | 4.30e-89 | 32 | 403 | 8 | 360 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
3A5V_A | 8.84e-76 | 29 | 384 | 5 | 371 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B3PGJ1 | 1.28e-95 | 1 | 391 | 1 | 378 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
Q8RX86 | 8.05e-92 | 29 | 396 | 36 | 384 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
Q9FXT4 | 4.27e-91 | 17 | 403 | 48 | 414 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
Q42656 | 1.04e-90 | 17 | 403 | 4 | 375 | Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1 |
P14749 | 2.25e-89 | 19 | 379 | 42 | 383 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000214 | 0.999182 | 0.000149 | 0.000166 | 0.000144 | 0.000132 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.