| Species | Eubacterium_R sp900539845 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900539845 | |||||||||||
| CAZyme ID | MGYG000002232_01740 | |||||||||||
| CAZy Family | GH27 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 18679; End: 20409 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH27 | 328 | 551 | 2.6e-58 | 0.8296943231441049 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd14792 | GH27 | 2.29e-108 | 63 | 481 | 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 | 3.64e-87 | 56 | 576 | 25 | 386 | alpha-galactosidase |
| PLN02692 | PLN02692 | 9.20e-79 | 44 | 571 | 37 | 406 | alpha-galactosidase |
| PLN02229 | PLN02229 | 3.26e-74 | 57 | 576 | 57 | 420 | alpha-galactosidase |
| pfam16499 | Melibiase_2 | 1.14e-61 | 62 | 481 | 1 | 284 | Alpha galactosidase A. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AQS55991.1 | 3.53e-108 | 46 | 573 | 27 | 532 |
| QOR76597.1 | 1.86e-81 | 57 | 573 | 37 | 392 |
| QKV75375.1 | 2.60e-81 | 39 | 574 | 10 | 386 |
| UAC00908.1 | 5.95e-79 | 56 | 574 | 38 | 398 |
| ADJ43732.1 | 1.34e-78 | 57 | 573 | 26 | 384 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1UAS_A | 2.66e-68 | 55 | 571 | 1 | 357 | ChainA, alpha-galactosidase [Oryza sativa] |
| 3A5V_A | 1.96e-59 | 57 | 552 | 3 | 367 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
| 4OGZ_A | 2.41e-57 | 28 | 521 | 62 | 423 | 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] |
| 6F4C_B | 3.26e-57 | 56 | 571 | 2 | 358 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
| 4NZJ_A | 3.66e-57 | 62 | 575 | 99 | 475 | Crystalstructure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8RX86 | 5.46e-72 | 57 | 576 | 34 | 394 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
| P14749 | 2.88e-67 | 57 | 571 | 50 | 405 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
| Q9FXT4 | 6.63e-67 | 55 | 571 | 56 | 412 | Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1 |
| Q9FT97 | 1.59e-65 | 57 | 571 | 48 | 404 | Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 SV=1 |
| Q2UJ97 | 7.97e-62 | 57 | 567 | 24 | 432 | Probable alpha-galactosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aglB PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000072 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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