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CAZyme Information: MGYG000002285_00457

You are here: Home > Sequence: MGYG000002285_00457

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 CAG-95 sp900066375
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-95; CAG-95 sp900066375
CAZyme ID MGYG000002285_00457
CAZy Family CE17
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
374 MGYG000002285_2|CGC2 42152.6 4.6624
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002285 3374269 Isolate China Asia
Gene Location Start: 86312;  End: 87436  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002285_00457.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE17 37 200 5.2e-76 0.9939393939393939
CBM35inCE17 227 373 2.4e-58 0.9798657718120806

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00229 SGNH_hydrolase 3.62e-22 37 209 3 187
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 7.39e-20 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 8.34e-19 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 4.76e-09 37 218 13 216
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd01822 Lysophospholipase_L1_like 7.03e-09 38 211 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 1.04e-159 1 373 1 370
EEV02614.1 4.23e-152 1 373 1 369
CBL10432.1 1.71e-151 1 373 1 369
CBL12377.1 1.71e-151 1 373 1 369
AEN97394.1 2.42e-140 1 373 1 381

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6HH9_A 1.90e-153 1 373 1 369
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 4.16e-150 2 373 2 369
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]
5TIC_A 1.76e-08 38 203 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]
5TID_A 1.76e-08 38 203 10 170
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]
1IVN_A 1.90e-08 38 203 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 1.34e-07 38 203 33 193
Thioesterase 1/protease 1/lysophospholipase L1 OS=Escherichia coli (strain K12) OX=83333 GN=tesA PE=1 SV=1
P0ADA2 1.34e-07 38 203 33 193
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
1.000056 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002285_00457.