Species | Coprobacter secundus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Coprobacteraceae; Coprobacter; Coprobacter secundus | |||||||||||
CAZyme ID | MGYG000001512_02140 | |||||||||||
CAZy Family | GH27 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 93200; End: 94666 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 216 | 467 | 2.8e-82 | 0.982532751091703 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 1.37e-147 | 120 | 403 | 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 | 1.64e-122 | 112 | 487 | 24 | 383 | alpha-galactosidase |
PLN02692 | PLN02692 | 3.00e-115 | 114 | 488 | 50 | 409 | alpha-galactosidase |
PLN02229 | PLN02229 | 3.11e-112 | 105 | 486 | 48 | 416 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 2.27e-98 | 119 | 403 | 1 | 284 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCI63984.1 | 0.0 | 1 | 488 | 1 | 488 |
VDS02529.1 | 1.56e-199 | 28 | 488 | 20 | 484 |
VDS02573.1 | 2.56e-199 | 28 | 488 | 34 | 498 |
QRM68960.1 | 2.34e-194 | 28 | 488 | 31 | 496 |
QCQ52869.1 | 2.34e-194 | 28 | 488 | 31 | 496 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4OGZ_A | 9.72e-187 | 28 | 488 | 8 | 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] |
4NZJ_A | 1.05e-184 | 28 | 486 | 8 | 472 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
1UAS_A | 5.47e-109 | 114 | 487 | 3 | 359 | ChainA, alpha-galactosidase [Oryza sativa] |
6F4C_B | 1.86e-92 | 112 | 487 | 1 | 360 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
3A5V_A | 1.66e-90 | 114 | 481 | 3 | 384 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9FXT4 | 1.75e-107 | 114 | 487 | 58 | 414 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
P14749 | 4.60e-106 | 87 | 487 | 23 | 407 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q9FT97 | 2.00e-104 | 114 | 488 | 48 | 407 | Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 SV=1 |
Q8RX86 | 4.08e-103 | 112 | 487 | 32 | 391 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
Q8VXZ7 | 7.33e-103 | 110 | 487 | 63 | 427 | Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000414 | 0.998294 | 0.000756 | 0.000183 | 0.000174 | 0.000166 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.