Species | Dysgonomonas mossii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae; Dysgonomonas; Dysgonomonas mossii | |||||||||||
CAZyme ID | MGYG000001377_02545 | |||||||||||
CAZy Family | CBM51 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 152609; End: 154603 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH27 | 377 | 640 | 4.4e-72 | 0.982532751091703 |
CBM51 | 38 | 164 | 6.4e-33 | 0.9328358208955224 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14792 | GH27 | 1.01e-117 | 283 | 560 | 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 | 3.53e-85 | 275 | 663 | 24 | 386 | alpha-galactosidase |
PLN02229 | PLN02229 | 1.93e-82 | 279 | 662 | 59 | 419 | alpha-galactosidase |
PLN02692 | PLN02692 | 1.73e-76 | 261 | 662 | 32 | 410 | alpha-galactosidase |
pfam16499 | Melibiase_2 | 1.13e-68 | 282 | 560 | 1 | 284 | Alpha galactosidase A. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT65548.1 | 0.0 | 10 | 664 | 1 | 655 |
QUT97956.1 | 0.0 | 10 | 664 | 1 | 655 |
ALJ57993.1 | 0.0 | 12 | 662 | 12 | 662 |
QUT90877.1 | 0.0 | 12 | 662 | 12 | 662 |
QBJ19564.1 | 0.0 | 19 | 664 | 19 | 664 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4OGZ_A | 6.29e-93 | 196 | 588 | 13 | 415 | 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 | 2.43e-89 | 196 | 592 | 13 | 419 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
1UAS_A | 1.35e-72 | 279 | 662 | 5 | 361 | ChainA, alpha-galactosidase [Oryza sativa] |
3A5V_A | 5.38e-71 | 279 | 659 | 5 | 389 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
6F4C_B | 1.19e-68 | 275 | 663 | 1 | 363 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14749 | 1.06e-78 | 279 | 663 | 52 | 410 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
Q55B10 | 2.55e-73 | 279 | 662 | 24 | 383 | Probable alpha-galactosidase OS=Dictyostelium discoideum OX=44689 GN=melA PE=3 SV=1 |
Q8VXZ7 | 2.98e-72 | 274 | 662 | 64 | 429 | Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1 |
Q8RX86 | 3.66e-72 | 279 | 664 | 36 | 395 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
Q9FXT4 | 3.52e-71 | 279 | 662 | 60 | 416 | 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 |
---|---|---|---|---|---|
0.000003 | 0.001755 | 0.998312 | 0.000001 | 0.000001 | 0.000001 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.