Species | Parabacteroides timonensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides timonensis | |||||||||||
CAZyme ID | MGYG000001591_02917 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Alpha-galactosidase A | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 17178; End: 18410 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 137 | 386 | 1.5e-89 | 0.9868995633187773 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 5.34e-154 | 42 | 311 | 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 | 2.84e-137 | 36 | 409 | 26 | 386 | alpha-galactosidase |
PLN02692 | PLN02692 | 3.88e-131 | 36 | 385 | 50 | 386 | alpha-galactosidase |
PLN02229 | PLN02229 | 3.01e-129 | 36 | 385 | 57 | 395 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 1.74e-101 | 41 | 311 | 1 | 284 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ALK83491.1 | 3.98e-266 | 2 | 410 | 8 | 416 |
BBE17165.1 | 5.60e-225 | 35 | 410 | 24 | 399 |
QUT97958.1 | 3.13e-198 | 36 | 410 | 24 | 397 |
QUT65546.1 | 3.13e-198 | 36 | 410 | 24 | 397 |
QBJ19567.1 | 3.84e-186 | 36 | 409 | 24 | 399 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1UAS_A | 1.67e-109 | 36 | 408 | 3 | 361 | ChainA, alpha-galactosidase [Oryza sativa] |
3A5V_A | 1.47e-108 | 36 | 405 | 3 | 389 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
6F4C_B | 3.94e-108 | 36 | 409 | 3 | 363 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
4OGZ_A | 7.02e-103 | 26 | 345 | 84 | 420 | 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 | 7.05e-101 | 28 | 345 | 86 | 420 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B3PGJ1 | 8.36e-158 | 29 | 409 | 20 | 404 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
P14749 | 8.60e-119 | 36 | 409 | 50 | 410 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q8RX86 | 2.76e-116 | 36 | 410 | 34 | 395 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
Q9FT97 | 9.92e-115 | 36 | 385 | 48 | 384 | Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 SV=1 |
Q8VXZ7 | 2.14e-112 | 36 | 409 | 67 | 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 |
---|---|---|---|---|---|
0.000227 | 0.999151 | 0.000146 | 0.000155 | 0.000142 | 0.000136 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.