| Species | UMGS1696 sp900554225 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS1696; UMGS1696 sp900554225 | |||||||||||
| CAZyme ID | MGYG000000468_01677 | |||||||||||
| CAZy Family | GH27 | |||||||||||
| CAZyme Description | Alpha-galactosidase A | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 16034; End: 17167 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH27 | 101 | 351 | 4.3e-64 | 0.9868995633187773 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd14792 | GH27 | 4.66e-140 | 6 | 278 | 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 | 2.55e-105 | 2 | 373 | 28 | 384 | alpha-galactosidase |
| PLN02229 | PLN02229 | 1.25e-100 | 2 | 370 | 59 | 415 | alpha-galactosidase |
| PLN02692 | PLN02692 | 1.75e-92 | 2 | 370 | 52 | 406 | alpha-galactosidase |
| pfam16499 | Melibiase_2 | 3.25e-91 | 6 | 278 | 2 | 284 | Alpha galactosidase A. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AEE96273.1 | 1.17e-158 | 1 | 374 | 1 | 374 |
| QAA34453.1 | 1.79e-157 | 1 | 371 | 1 | 369 |
| QTE68632.1 | 7.67e-152 | 1 | 374 | 1 | 391 |
| QUA53570.1 | 7.71e-150 | 1 | 374 | 3 | 393 |
| AIQ57865.1 | 1.51e-149 | 2 | 374 | 7 | 386 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1UAS_A | 3.45e-89 | 2 | 373 | 5 | 360 | ChainA, alpha-galactosidase [Oryza sativa] |
| 6F4C_B | 1.15e-84 | 2 | 373 | 5 | 361 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
| 4OGZ_A | 3.00e-82 | 2 | 372 | 96 | 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] |
| 3A5V_A | 1.76e-80 | 2 | 371 | 5 | 389 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
| 4NZJ_A | 6.33e-79 | 2 | 311 | 96 | 419 | 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 |
|---|---|---|---|---|---|---|
| P14749 | 8.15e-94 | 2 | 373 | 52 | 408 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
| Q9FXT4 | 9.90e-88 | 2 | 373 | 60 | 415 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
| Q8RX86 | 4.23e-87 | 2 | 373 | 36 | 392 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
| Q8VXZ7 | 1.11e-85 | 2 | 373 | 69 | 428 | Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1 |
| Q42656 | 3.13e-82 | 2 | 373 | 20 | 376 | Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.952963 | 0.045554 | 0.000867 | 0.000200 | 0.000105 | 0.000334 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.