| Species | Phocaeicola plebeius | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola plebeius | |||||||||||
| CAZyme ID | MGYG000001364_02431 | |||||||||||
| CAZy Family | GH27 | |||||||||||
| CAZyme Description | Alpha-galactosidase A | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 41651; End: 42880 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH27 | 137 | 385 | 9.5e-90 | 0.982532751091703 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd14792 | GH27 | 3.52e-156 | 42 | 311 | 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 | 9.47e-140 | 36 | 407 | 26 | 384 | alpha-galactosidase |
| PLN02692 | PLN02692 | 5.96e-132 | 36 | 385 | 50 | 386 | alpha-galactosidase |
| PLN02229 | PLN02229 | 4.80e-129 | 36 | 385 | 57 | 395 | alpha-galactosidase |
| pfam16499 | Melibiase_2 | 2.87e-101 | 41 | 311 | 1 | 284 | Alpha galactosidase A. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ALK83491.1 | 3.34e-260 | 20 | 407 | 26 | 413 |
| BBE17165.1 | 2.67e-225 | 22 | 408 | 11 | 397 |
| QUT97958.1 | 2.10e-191 | 36 | 409 | 24 | 396 |
| QUT65546.1 | 2.10e-191 | 36 | 409 | 24 | 396 |
| QBJ19567.1 | 8.16e-183 | 36 | 409 | 24 | 399 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1UAS_A | 3.84e-113 | 36 | 407 | 3 | 360 | ChainA, alpha-galactosidase [Oryza sativa] |
| 6F4C_B | 2.94e-110 | 36 | 409 | 3 | 363 | Nicotianabenthamiana alpha-galactosidase [Nicotiana benthamiana] |
| 3A5V_A | 3.54e-109 | 36 | 405 | 3 | 389 | Crystalstructure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea] |
| 4OGZ_A | 7.63e-102 | 26 | 345 | 84 | 420 | 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 | 3.41e-98 | 26 | 348 | 84 | 423 | 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 |
|---|---|---|---|---|---|---|
| B3PGJ1 | 1.33e-151 | 4 | 407 | 3 | 402 | Alpha-galactosidase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agaA PE=1 SV=1 |
| P14749 | 2.44e-123 | 36 | 407 | 50 | 408 | Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1 |
| Q8RX86 | 7.84e-121 | 36 | 407 | 34 | 392 | Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1 |
| Q9FT97 | 2.60e-117 | 36 | 385 | 48 | 384 | Alpha-galactosidase 1 OS=Arabidopsis thaliana OX=3702 GN=AGAL1 PE=2 SV=1 |
| Q55B10 | 1.50e-115 | 18 | 407 | 4 | 382 | Probable alpha-galactosidase OS=Dictyostelium discoideum OX=44689 GN=melA PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.005534 | 0.855378 | 0.138268 | 0.000309 | 0.000261 | 0.000232 |
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