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CAZyme Information: MGYG000002256_01348
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA3282; | |||||||||||
| CAZyme ID | MGYG000002256_01348 | |||||||||||
| CAZy Family | CE17 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 16268; End: 17389 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE17 | 38 | 201 | 1e-75 | 0.9939393939393939 |
| CBM35inCE17 | 228 | 372 | 2.6e-58 | 0.9664429530201343 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd00229 | SGNH_hydrolase | 7.19e-22 | 36 | 210 | 1 | 187 | 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. |
| pfam13472 | Lipase_GDSL_2 | 3.18e-20 | 38 | 202 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| cd01834 | SGNH_hydrolase_like_2 | 2.71e-15 | 31 | 206 | 1 | 187 | 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. |
| PRK10528 | PRK10528 | 9.67e-09 | 24 | 204 | 3 | 176 | multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional |
| cd01822 | Lysophospholipase_L1_like | 2.35e-08 | 39 | 212 | 6 | 177 | Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BCN32107.1 | 1.73e-148 | 9 | 372 | 8 | 370 |
| EEV02614.1 | 1.71e-141 | 6 | 372 | 5 | 369 |
| CBL10432.1 | 5.63e-140 | 6 | 372 | 5 | 369 |
| CBL12377.1 | 5.63e-140 | 6 | 372 | 5 | 369 |
| AEN97394.1 | 8.85e-133 | 6 | 372 | 5 | 381 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6HH9_A | 7.69e-143 | 6 | 372 | 5 | 369 | 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 | 4.13e-140 | 6 | 372 | 5 | 369 | 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] |
| 6LFC_A | 2.58e-07 | 39 | 204 | 7 | 167 | E.coli Thioesterase I mutant DG [Escherichia coli],6LFC_B E. coli Thioesterase I mutant DG [Escherichia coli],6LFC_C E. coli Thioesterase I mutant DG [Escherichia coli],6LFC_D E. coli Thioesterase I mutant DG [Escherichia coli],6LFC_E E. coli Thioesterase I mutant DG [Escherichia coli],6LFC_F E. coli Thioesterase I mutant DG [Escherichia coli] |
| 5TIC_A | 2.70e-07 | 39 | 204 | 10 | 170 | X-raystructure of wild-type E. coli Acyl-CoA thioesterase I at pH 5 [Escherichia coli],5TIC_B X-ray structure of wild-type E. coli Acyl-CoA thioesterase I at pH 5 [Escherichia coli] |
| 1IVN_A | 2.89e-07 | 39 | 204 | 7 | 167 | E.coliThioesterase I/Protease I/Lysophospholiase L1 [Escherichia coli],1U8U_A E. coli Thioesterase I/Protease I/Lysophospholiase L1 in complexed with octanoic acid [Escherichia coli] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P0ADA1 | 5.98e-07 | 27 | 204 | 23 | 193 | Thioesterase 1/protease 1/lysophospholipase L1 OS=Escherichia coli (strain K12) OX=83333 GN=tesA PE=1 SV=1 |
| P0ADA2 | 5.98e-07 | 27 | 204 | 23 | 193 | Thioesterase 1/protease 1/lysophospholipase L1 OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=tesA PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000035 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |