Species | CAG-475 sp900547975 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-917; CAG-475; CAG-475 sp900547975 | |||||||||||
CAZyme ID | MGYG000003849_01434 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 44256; End: 45881 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 306 | 517 | 1.5e-60 | 0.8253275109170306 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 3.38e-106 | 39 | 448 | 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 | 5.14e-88 | 32 | 540 | 25 | 383 | alpha-galactosidase |
PLN02692 | PLN02692 | 5.36e-85 | 33 | 541 | 50 | 409 | alpha-galactosidase |
PLN02229 | PLN02229 | 3.34e-82 | 32 | 539 | 56 | 416 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 5.96e-65 | 38 | 448 | 1 | 284 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AQS55991.1 | 1.22e-118 | 32 | 541 | 39 | 533 |
QOR76597.1 | 6.13e-84 | 9 | 526 | 19 | 378 |
QEE25737.1 | 7.24e-78 | 32 | 530 | 28 | 385 |
QHA10193.1 | 9.79e-78 | 33 | 530 | 36 | 381 |
BBE17165.1 | 2.18e-77 | 35 | 513 | 27 | 355 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1UAS_A | 7.81e-70 | 31 | 539 | 1 | 358 | ChainA, alpha-galactosidase [Oryza sativa] |
6F4C_B | 6.41e-63 | 33 | 539 | 3 | 359 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
4OGZ_A | 1.70e-52 | 35 | 495 | 96 | 434 | 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 | 1.85e-52 | 35 | 539 | 96 | 472 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
3A5V_A | 6.06e-52 | 32 | 487 | 2 | 336 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14749 | 3.28e-73 | 15 | 539 | 27 | 406 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q8RX86 | 9.68e-71 | 32 | 486 | 33 | 342 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
Q9FT97 | 2.14e-69 | 33 | 541 | 48 | 407 | Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 SV=1 |
Q9FXT4 | 1.96e-68 | 31 | 539 | 56 | 413 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
B3PGJ1 | 5.35e-68 | 35 | 530 | 29 | 391 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000066 | 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.