| Species | Parabacteroides merdae | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides merdae | |||||||||||
| CAZyme ID | MGYG000000044_02771 | |||||||||||
| CAZy Family | CE17 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 325490; End: 327442 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE17 | 305 | 471 | 3.5e-16 | 0.9878787878787879 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam13472 | Lipase_GDSL_2 | 3.97e-13 | 305 | 472 | 1 | 175 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| cd00229 | SGNH_hydrolase | 1.52e-11 | 303 | 478 | 1 | 184 | SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. |
| cd01834 | SGNH_hydrolase_like_2 | 3.47e-06 | 302 | 373 | 3 | 73 | SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. |
| COG1506 | DAP2 | 1.90e-05 | 79 | 272 | 412 | 616 | Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]. |
| pfam00561 | Abhydrolase_1 | 3.15e-05 | 76 | 170 | 10 | 110 | alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AEE54090.1 | 1.82e-152 | 40 | 648 | 396 | 1015 |
| QEC52777.1 | 1.23e-82 | 277 | 648 | 816 | 1251 |
| BAV07942.1 | 4.92e-68 | 274 | 649 | 22 | 394 |
| AHF91789.1 | 4.46e-28 | 285 | 608 | 40 | 377 |
| AXT62271.1 | 2.75e-22 | 284 | 647 | 35 | 394 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6HH9_A | 1.60e-15 | 303 | 571 | 35 | 291 | Crystalstructure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82] |
| 6HFZ_A | 5.09e-15 | 303 | 571 | 35 | 291 | Crystalstructure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82] |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.003259 | 0.995903 | 0.000289 | 0.000194 | 0.000162 | 0.000167 |
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