Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UMGS2037; | |||||||||||
CAZyme ID | MGYG000003578_03280 | |||||||||||
CAZy Family | CE17 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 9419; End: 10546 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE17 | 37 | 200 | 5.7e-73 | 0.9939393939393939 |
CBM35inCE17 | 228 | 374 | 2.9e-59 | 0.9798657718120806 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00229 | SGNH_hydrolase | 9.33e-21 | 35 | 209 | 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 | 7.53e-19 | 37 | 201 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
cd01834 | SGNH_hydrolase_like_2 | 6.03e-17 | 37 | 206 | 6 | 188 | 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. |
COG2755 | TesA | 1.86e-08 | 25 | 210 | 1 | 208 | Lysophospholipase L1 or related esterase [Amino acid transport and metabolism]. |
cd01822 | Lysophospholipase_L1_like | 7.06e-08 | 34 | 210 | 2 | 176 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCN32107.1 | 1.43e-169 | 1 | 374 | 1 | 370 |
CBL10432.1 | 9.38e-154 | 1 | 375 | 1 | 370 |
CBL12377.1 | 9.38e-154 | 1 | 375 | 1 | 370 |
EEV02614.1 | 9.38e-154 | 1 | 375 | 1 | 370 |
AEN97394.1 | 5.81e-139 | 1 | 374 | 1 | 381 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6HH9_A | 4.22e-155 | 1 | 375 | 1 | 370 | 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 | 3.74e-151 | 3 | 375 | 3 | 370 | 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] |
7DDY_A | 2.73e-06 | 24 | 203 | 15 | 213 | ChainA, G-D-S-L family lipolytic protein [Arcticibacterium luteifluviistationis],7DDY_B Chain B, G-D-S-L family lipolytic protein [Arcticibacterium luteifluviistationis],7DDY_C Chain C, G-D-S-L family lipolytic protein [Arcticibacterium luteifluviistationis],7DDY_D Chain D, G-D-S-L family lipolytic protein [Arcticibacterium luteifluviistationis] |
5TIC_A | 7.53e-06 | 34 | 203 | 6 | 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] |
5TID_A | 7.53e-06 | 34 | 203 | 6 | 170 | X-raystructure of acyl-CoA thioesterase I, TesA, mutant M141L/Y145K/L146K at pH 5 in complex with octanoic acid [Escherichia coli],5TIE_A x-ray structure of acyl-CoA thioesterase I, TesA, mutant M141L/Y145K/L146K at pH 7.5 in complex with octanoic acid [Escherichia coli],5TIF_A x-ray structure of acyl-CoA thioesterase I, TesA, triple mutant M141L/Y145K/L146K in complex with octanoic acid [Escherichia coli] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000023 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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