| Species | Blautia_A faecis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A faecis | |||||||||||
| CAZyme ID | MGYG000000002_00460 | |||||||||||
| CAZy Family | GH27 | |||||||||||
| CAZyme Description | Alpha-galactosidase A | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 527770; End: 528915 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH27 | 101 | 341 | 2e-58 | 0.9432314410480349 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd14792 | GH27 | 1.42e-129 | 8 | 279 | 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. |
| pfam16499 | Melibiase_2 | 3.75e-93 | 8 | 279 | 2 | 284 | Alpha galactosidase A. |
| PLN02808 | PLN02808 | 4.55e-93 | 4 | 337 | 28 | 349 | alpha-galactosidase |
| PLN02229 | PLN02229 | 1.76e-86 | 4 | 372 | 59 | 416 | alpha-galactosidase |
| PLN02692 | PLN02692 | 1.10e-81 | 4 | 342 | 52 | 378 | alpha-galactosidase |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QTE71472.1 | 2.03e-141 | 3 | 376 | 4 | 395 |
| QTE75438.1 | 2.03e-141 | 3 | 376 | 4 | 395 |
| QUC67774.1 | 4.71e-140 | 3 | 376 | 4 | 395 |
| QUA53570.1 | 5.24e-139 | 1 | 376 | 1 | 394 |
| QTE68632.1 | 5.63e-138 | 3 | 376 | 1 | 392 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4NZJ_A | 7.19e-79 | 4 | 372 | 96 | 472 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
| 4OGZ_A | 5.06e-78 | 4 | 374 | 96 | 473 | 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] |
| 1UAS_A | 2.78e-74 | 4 | 372 | 5 | 358 | ChainA, alpha-galactosidase [Oryza sativa] |
| 6F4C_B | 5.70e-74 | 4 | 342 | 5 | 331 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
| 3A5V_A | 3.29e-72 | 4 | 309 | 5 | 326 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| B3PGJ1 | 1.52e-81 | 4 | 320 | 29 | 345 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
| P14749 | 1.86e-81 | 4 | 342 | 52 | 378 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
| Q8RX86 | 8.42e-79 | 4 | 313 | 36 | 336 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
| Q42656 | 1.71e-73 | 4 | 313 | 20 | 320 | Alpha-galactosidase OS=Coffea arabica OX=13443 PE=1 SV=1 |
| Q9FXT4 | 7.15e-73 | 4 | 372 | 60 | 413 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000066 | 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.