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CAZyme Information: MGYG000000389_00051

You are here: Home > Sequence: MGYG000000389_00051

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 Roseburia sp900550935
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia sp900550935
CAZyme ID MGYG000000389_00051
CAZy Family CE17
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
371 MGYG000000389_1|CGC1 41622.08 5.0041
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000389 2762523 MAG Sweden Europe
Gene Location Start: 58328;  End: 59443  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000389_00051.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE17 37 200 4.3e-80 0.9939393939393939
CBM35inCE17 225 370 5.3e-59 0.9731543624161074

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00229 SGNH_hydrolase 4.41e-24 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 1.01e-18 37 200 1 175
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd01834 SGNH_hydrolase_like_2 8.81e-15 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.
cd01822 Lysophospholipase_L1_like 1.89e-09 38 203 6 169
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.
COG2755 TesA 9.43e-08 32 206 8 208
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
EEV02614.1 2.34e-172 1 371 1 369
CBL10432.1 1.91e-171 1 371 1 369
CBL12377.1 1.91e-171 1 371 1 369
AEN97394.1 1.45e-167 1 371 1 381
BCN32107.1 4.58e-148 1 371 1 370

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6HH9_A 1.06e-173 1 371 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 3.32e-170 2 371 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 3.00e-06 30 179 2 133
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 3.00e-06 30 179 2 133
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]

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.997611 0.002290 0.000097 0.000004 0.000003 0.000006

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000389_00051.