Species | Prevotella veroralis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella veroralis | |||||||||||
CAZyme ID | MGYG000002636_00753 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Alpha-galactosidase A | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 24730; End: 25962 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 128 | 380 | 1e-83 | 0.9737991266375546 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 1.18e-152 | 33 | 304 | 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 | 3.39e-124 | 29 | 359 | 28 | 350 | alpha-galactosidase |
PLN02229 | PLN02229 | 9.36e-122 | 21 | 377 | 51 | 390 | alpha-galactosidase |
PLN02692 | PLN02692 | 4.00e-113 | 29 | 354 | 52 | 369 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 5.38e-102 | 32 | 304 | 1 | 284 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUB41946.1 | 2.10e-312 | 1 | 410 | 1 | 410 |
QUB47766.1 | 4.92e-267 | 3 | 409 | 1 | 407 |
VEH15502.1 | 5.48e-264 | 3 | 409 | 1 | 407 |
QUB71325.1 | 2.33e-254 | 3 | 410 | 1 | 408 |
BBL06472.1 | 8.26e-182 | 23 | 407 | 19 | 401 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1UAS_A | 4.94e-106 | 27 | 354 | 3 | 322 | ChainA, alpha-galactosidase [Oryza sativa] |
6F4C_B | 7.94e-97 | 27 | 359 | 3 | 327 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
4OGZ_A | 6.93e-94 | 27 | 348 | 94 | 430 | 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 | 4.84e-92 | 27 | 348 | 94 | 430 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
3A5V_A | 4.13e-91 | 27 | 409 | 3 | 389 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B3PGJ1 | 6.80e-157 | 15 | 407 | 15 | 401 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
Q8RX86 | 1.56e-107 | 21 | 371 | 28 | 370 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
Q55B10 | 3.10e-107 | 27 | 378 | 22 | 354 | Probable alpha-galactosidase OS=Dictyostelium discoideum OX=44689 GN=melA PE=3 SV=1 |
P14749 | 5.68e-106 | 20 | 354 | 43 | 369 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q9FXT4 | 1.10e-104 | 22 | 354 | 53 | 377 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000195 | 0.999162 | 0.000164 | 0.000154 | 0.000146 | 0.000131 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.