Species | Bacteroides ndongoniae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides ndongoniae | |||||||||||
CAZyme ID | MGYG000002621_02312 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Alpha-galactosidase A | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 22538; End: 23641 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 80 | 343 | 5e-69 | 0.982532751091703 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 1.84e-94 | 16 | 263 | 32 | 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 | 3.75e-64 | 16 | 366 | 63 | 386 | alpha-galactosidase |
PLN02229 | PLN02229 | 1.65e-62 | 16 | 365 | 94 | 419 | alpha-galactosidase |
PLN02692 | PLN02692 | 4.39e-59 | 16 | 366 | 87 | 411 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 1.75e-54 | 20 | 263 | 47 | 284 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QDO70844.1 | 4.15e-212 | 14 | 365 | 309 | 660 |
ALJ57993.1 | 8.36e-210 | 14 | 366 | 311 | 663 |
QUT90877.1 | 4.79e-209 | 14 | 366 | 311 | 663 |
BBL13308.1 | 5.07e-200 | 11 | 366 | 303 | 658 |
BBL10514.1 | 5.07e-200 | 11 | 366 | 303 | 658 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1UAS_A | 7.95e-59 | 16 | 365 | 40 | 361 | ChainA, alpha-galactosidase [Oryza sativa] |
3A5V_A | 1.24e-55 | 16 | 362 | 40 | 389 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
6F4C_B | 4.75e-53 | 16 | 365 | 40 | 362 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
4NZJ_A | 8.26e-53 | 20 | 333 | 135 | 460 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
4OGZ_A | 1.49e-52 | 20 | 291 | 135 | 415 | 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 |
---|---|---|---|---|---|---|
P14749 | 6.53e-60 | 16 | 365 | 87 | 409 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q55B10 | 1.44e-58 | 20 | 365 | 63 | 383 | Probable alpha-galactosidase OS=Dictyostelium discoideum OX=44689 GN=melA PE=3 SV=1 |
Q9FXT4 | 1.74e-57 | 16 | 365 | 95 | 416 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
Q8VXZ7 | 7.73e-57 | 16 | 365 | 104 | 429 | Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1 |
Q8RX86 | 1.30e-54 | 16 | 360 | 71 | 388 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000065 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.