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CAZyme Information: MGYG000000334_00828

You are here: Home > Sequence: MGYG000000334_00828

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; Oscillospirales; Oscillospiraceae; UBA5446;
CAZyme ID MGYG000000334_00828
CAZy Family CE17
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
451 MGYG000000334_88|CGC1 50550.26 4.743
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000334 2196649 MAG Sweden Europe
Gene Location Start: 4251;  End: 5606  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000334_00828.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE17 104 277 1.3e-31 0.9878787878787879

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam13472 Lipase_GDSL_2 5.10e-12 104 279 1 176
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd00229 SGNH_hydrolase 1.14e-11 102 284 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.
pfam00657 Lipase_GDSL 1.77e-05 102 284 1 224
GDSL-like Lipase/Acylhydrolase.
COG2755 TesA 3.25e-04 101 282 10 202
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd01834 SGNH_hydrolase_like_2 0.002 102 280 4 184
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QSF46877.1 4.01e-152 6 449 129 576
QYK61360.1 3.33e-151 6 451 130 579
BCJ92770.1 1.86e-33 72 403 5 318
BCN32107.1 2.02e-31 70 442 3 359
EEV02614.1 2.06e-31 76 398 14 310

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6HH9_A 8.36e-33 76 398 14 310
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 2.19e-32 76 398 14 310
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]

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
1.000039 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000334_00828.