Species | Bacteroides sp014385165 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp014385165 | |||||||||||
CAZyme ID | MGYG000003922_02219 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 13443; End: 14945 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 219 | 469 | 1.4e-78 | 0.9563318777292577 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 2.35e-142 | 123 | 410 | 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 | 3.52e-113 | 97 | 494 | 6 | 382 | alpha-galactosidase |
PLN02692 | PLN02692 | 2.94e-101 | 115 | 447 | 48 | 356 | alpha-galactosidase |
PLN02229 | PLN02229 | 4.92e-100 | 113 | 451 | 53 | 369 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 4.12e-92 | 122 | 410 | 1 | 284 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ALJ39654.1 | 3.29e-289 | 14 | 497 | 15 | 500 |
QQA08762.1 | 3.29e-289 | 14 | 497 | 15 | 500 |
BCA52401.1 | 3.29e-289 | 14 | 497 | 15 | 500 |
AAO78171.1 | 1.34e-288 | 14 | 497 | 15 | 500 |
QMW85489.1 | 1.34e-288 | 14 | 497 | 15 | 500 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4OGZ_A | 3.61e-266 | 32 | 495 | 9 | 472 | 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 | 5.94e-266 | 32 | 497 | 9 | 475 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
1UAS_A | 2.33e-96 | 122 | 494 | 8 | 358 | ChainA, alpha-galactosidase [Oryza sativa] |
6F4C_B | 7.87e-85 | 122 | 494 | 8 | 359 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
3A5V_A | 2.27e-80 | 119 | 447 | 5 | 333 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14749 | 1.89e-99 | 122 | 494 | 55 | 406 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
B3PGJ1 | 5.35e-97 | 117 | 450 | 27 | 344 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
Q9FXT4 | 7.02e-95 | 122 | 494 | 63 | 413 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
Q8RX86 | 1.82e-92 | 115 | 493 | 32 | 389 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
Q55B10 | 1.14e-90 | 115 | 487 | 20 | 383 | Probable alpha-galactosidase OS=Dictyostelium discoideum OX=44689 GN=melA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000934 | 0.997993 | 0.000476 | 0.000230 | 0.000166 | 0.000170 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.