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CAZyme Information: MGYG000001370_01658

You are here: Home > Sequence: MGYG000001370_01658

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 Bacteroides fluxus
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides fluxus
CAZyme ID MGYG000001370_01658
CAZy Family CE3
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
422 MGYG000001370_29|CGC2 47604.16 6.497
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001370 4330086 Isolate not provided not provided
Gene Location Start: 48716;  End: 49984  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001370_01658.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE3 197 417 5.8e-18 0.9845360824742269

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam03629 SASA 3.41e-40 23 192 3 226
Carbohydrate esterase, sialic acid-specific acetylesterase. The catalytic triad of this esterase enzyme comprises residues Ser127, His403 and Asp391 in UniProtKB:P70665.
cd01834 SGNH_hydrolase_like_2 1.53e-39 196 417 1 190
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.
pfam13472 Lipase_GDSL_2 3.11e-27 201 410 1 176
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd00229 SGNH_hydrolase 9.86e-21 199 417 1 186
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.
COG2755 TesA 2.15e-16 198 422 10 211
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
QUT78436.1 4.26e-46 21 192 30 260
QDM11351.1 4.26e-46 21 192 30 260
QRM98824.1 4.26e-46 21 192 30 260
QUT32559.1 5.97e-46 5 192 10 260
QDH54197.1 8.38e-46 22 192 31 260

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4Q9A_A 1.45e-29 199 421 22 228
Crystalstructure of a putative GDSL-like lipase (PARMER_00689) from Parabacteroides merdae ATCC 43184 at 2.86 A resolution [Parabacteroides merdae ATCC 43184],4Q9A_B Crystal structure of a putative GDSL-like lipase (PARMER_00689) from Parabacteroides merdae ATCC 43184 at 2.86 A resolution [Parabacteroides merdae ATCC 43184]
3W7V_A 7.89e-28 195 420 5 212
CrystalStructure of Axe2, an Acetylxylan Esterase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],3W7V_B Crystal Structure of Axe2, an Acetylxylan Esterase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
5BN1_A 7.89e-28 195 420 5 212
Structureof Axe2-W215I, an acetyl xylan esterase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5BN1_B Structure of Axe2-W215I, an acetyl xylan esterase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
4OAO_A 7.89e-28 195 420 5 212
Amutant of Axe2 (R55A), and acetyl-xylooligosaccharide esterase from Geobacillus Stearmophilus [Geobacillus stearothermophilus],4OAO_B A mutant of Axe2 (R55A), and acetyl-xylooligosaccharide esterase from Geobacillus Stearmophilus [Geobacillus stearothermophilus]
4JKO_A 2.09e-27 195 420 5 212
Crystalstructure of a catalytic mutant of Axe2 (Axe2_S15A), an acetylxylan esterase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4JKO_B Crystal structure of a catalytic mutant of Axe2 (Axe2_S15A), an acetylxylan esterase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q09LX1 4.32e-27 195 420 5 212
Acetylxylan esterase OS=Geobacillus stearothermophilus OX=1422 GN=axe2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000212 0.999198 0.000155 0.000142 0.000135 0.000133

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001370_01658.