Species | Eubacterium_F sp003491505 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_F; Eubacterium_F sp003491505 | |||||||||||
CAZyme ID | MGYG000000209_01063 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | Alpha-galactosidase A | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 153891; End: 155066 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 110 | 367 | 1.2e-68 | 0.9912663755458515 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 1.11e-134 | 16 | 292 | 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 | 1.77e-97 | 1 | 383 | 19 | 378 | alpha-galactosidase |
PLN02229 | PLN02229 | 5.23e-95 | 12 | 383 | 59 | 412 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 2.88e-93 | 16 | 292 | 2 | 284 | Alpha galactosidase A. |
PLN02692 | PLN02692 | 2.45e-92 | 9 | 383 | 49 | 403 | alpha-galactosidase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QOS76902.1 | 5.55e-238 | 8 | 391 | 3 | 386 |
APO43919.1 | 7.88e-238 | 8 | 391 | 3 | 386 |
QZN77867.1 | 1.59e-237 | 8 | 391 | 3 | 386 |
QLG36889.1 | 2.26e-237 | 5 | 391 | 1 | 386 |
QKS60285.1 | 7.28e-235 | 12 | 391 | 2 | 381 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1UAS_A | 1.75e-84 | 11 | 383 | 4 | 354 | ChainA, alpha-galactosidase [Oryza sativa] |
6F4C_B | 2.55e-81 | 9 | 383 | 2 | 355 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
4NZJ_A | 2.51e-79 | 16 | 341 | 100 | 429 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
4OGZ_A | 3.50e-78 | 16 | 385 | 100 | 469 | 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 | 4.20e-76 | 11 | 380 | 4 | 382 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14749 | 1.84e-84 | 5 | 383 | 47 | 402 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q8VXZ7 | 2.18e-83 | 11 | 383 | 68 | 422 | Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1 |
Q9FXT4 | 4.88e-83 | 11 | 383 | 59 | 409 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
Q8RX86 | 2.96e-82 | 11 | 383 | 35 | 386 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
Q42656 | 9.78e-82 | 11 | 382 | 19 | 369 | 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 |
---|---|---|---|---|---|
1.000074 | 0.000000 | 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.