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CAZyme Information: MGYG000001927_01942

You are here: Home > Sequence: MGYG000001927_01942

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 Prevotella sp900547005
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900547005
CAZyme ID MGYG000001927_01942
CAZy Family CE3
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
442 49705.76 8.7351
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001927 2803818 MAG Denmark Europe
Gene Location Start: 4014;  End: 5342  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001927_01942.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE3 32 220 1.1e-40 0.9845360824742269

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd01833 XynB_like 3.97e-27 30 220 1 157
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. 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 1.91e-15 35 211 2 176
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd00229 SGNH_hydrolase 5.85e-14 32 219 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.
COG2755 TesA 1.86e-11 31 226 10 214
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd01827 sialate_O-acetylesterase_like1 4.98e-11 35 220 6 187
sialate O-acetylesterase_like family of the SGNH hydrolases, 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
BAX78799.1 1.46e-109 25 441 33 494
ATC65549.1 1.60e-109 26 441 34 492
QOV88633.1 6.94e-66 28 227 28 229
QNN20991.1 1.34e-65 23 226 23 228
QRK14019.1 4.58e-27 33 224 1 199

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5AO9_A 1.71e-23 238 348 20 132
Thestructure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-native [Thermogutta terrifontis],5AOA_A The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-Propionate bound [Thermogutta terrifontis],5AOB_A The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-butyrate bound [Thermogutta terrifontis],5AOC_A The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-valerate bound [Thermogutta terrifontis]
7BFN_A 1.74e-23 238 348 21 133
ChainA, Esterase [Thermogutta terrifontis]
7BFO_A 8.37e-23 238 348 21 133
ChainA, Esterase [Thermogutta terrifontis],7BFR_A Chain A, Esterase [Thermogutta terrifontis],7BFT_A Chain A, Esterase [Thermogutta terrifontis],7BFU_A Chain A, Esterase [Thermogutta terrifontis],7BFV_A Chain A, Esterase [Thermogutta terrifontis]
2C7B_A 1.38e-08 246 365 59 186
TheCrystal Structure of EstE1, a New Thermophilic and Thermostable Carboxylesterase Cloned from a Metagenomic Library [uncultured archaeon],2C7B_B The Crystal Structure of EstE1, a New Thermophilic and Thermostable Carboxylesterase Cloned from a Metagenomic Library [uncultured archaeon]
5B5S_A 1.69e-08 32 213 4 192
Crystalstructure of a carbohydrate esterase family 3 from Talaromyces cellulolyticus [Talaromyces cellulolyticus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0A0G3FWY4 3.74e-10 249 351 62 162
Probable N-octanoylanthranilate hydrolase AqdA1 OS=Rhodococcus erythropolis OX=1833 GN=aqdA1 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
0.000198 0.999173 0.000164 0.000161 0.000155 0.000143

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001927_01942.