Species | Bacteroides uniformis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides uniformis | |||||||||||
CAZyme ID | MGYG000001346_03348 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Alpha-galactosidase A | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 984435; End: 985628 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 125 | 373 | 2.6e-93 | 0.9868995633187773 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 2.82e-161 | 30 | 299 | 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 | 1.04e-147 | 19 | 396 | 21 | 386 | alpha-galactosidase |
PLN02229 | PLN02229 | 2.89e-136 | 24 | 395 | 57 | 419 | alpha-galactosidase |
PLN02692 | PLN02692 | 1.20e-130 | 23 | 372 | 49 | 386 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 3.05e-106 | 29 | 299 | 1 | 284 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT97958.1 | 2.25e-314 | 1 | 397 | 1 | 397 |
QUT65546.1 | 1.85e-313 | 1 | 397 | 1 | 397 |
QBJ19567.1 | 1.55e-247 | 1 | 396 | 1 | 399 |
QMI80972.1 | 1.55e-247 | 1 | 396 | 1 | 399 |
ALK83491.1 | 1.70e-201 | 1 | 395 | 8 | 414 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1UAS_A | 1.49e-117 | 24 | 395 | 3 | 361 | ChainA, alpha-galactosidase [Oryza sativa] |
6F4C_B | 2.49e-116 | 23 | 396 | 2 | 363 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
3A5V_A | 2.76e-105 | 22 | 392 | 1 | 389 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
4NZJ_A | 1.02e-102 | 24 | 356 | 94 | 439 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
4OGZ_A | 1.28e-102 | 21 | 354 | 91 | 442 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B3PGJ1 | 2.09e-157 | 16 | 396 | 19 | 404 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
Q8RX86 | 6.50e-127 | 18 | 397 | 28 | 395 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
Q55B10 | 3.87e-123 | 11 | 395 | 8 | 383 | Probable alpha-galactosidase OS=Dictyostelium discoideum OX=44689 GN=melA PE=3 SV=1 |
P14749 | 1.29e-122 | 19 | 396 | 45 | 410 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q8VXZ7 | 5.05e-118 | 14 | 396 | 57 | 430 | Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000192 | 0.999182 | 0.000157 | 0.000160 | 0.000145 | 0.000135 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.