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CAZyme Information: MGYG000002281_00335

You are here: Home > Sequence: MGYG000002281_00335

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 faecis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides faecis
CAZyme ID MGYG000002281_00335
CAZy Family CE12
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
556 MGYG000002281_1|CGC8 62510.02 9.7547
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002281 6145961 Isolate China Asia
Gene Location Start: 483400;  End: 485070  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002281_00335.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE12 27 233 7.3e-70 0.9904761904761905
CE6 380 472 7e-28 0.98989898989899

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam03629 SASA 2.92e-86 319 548 1 222
Carbohydrate esterase, sialic acid-specific acetylesterase. The catalytic triad of this esterase enzyme comprises residues Ser127, His403 and Asp391 in UniProtKB:P70665.
cd01821 Rhamnogalacturan_acetylesterase_like 1.05e-81 27 234 2 198
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.
COG2755 TesA 3.99e-16 27 238 10 211
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
pfam13472 Lipase_GDSL_2 4.01e-15 31 225 2 176
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd00229 SGNH_hydrolase 2.71e-13 28 229 1 183
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCA48725.1 6.51e-171 306 556 17 267
QMW86523.1 5.29e-170 306 556 17 267
QUT69878.1 5.29e-170 306 556 17 267
AAO79285.1 5.29e-170 306 556 17 267
QUT42077.1 5.29e-170 306 556 17 267

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2APJ_A 1.03e-22 300 548 2 253
X-RayStructure of Protein from Arabidopsis Thaliana AT4G34215 at 1.6 Angstrom Resolution [Arabidopsis thaliana],2APJ_B X-Ray Structure of Protein from Arabidopsis Thaliana AT4G34215 at 1.6 Angstrom Resolution [Arabidopsis thaliana],2APJ_C X-Ray Structure of Protein from Arabidopsis Thaliana AT4G34215 at 1.6 Angstrom Resolution [Arabidopsis thaliana],2APJ_D X-Ray Structure of Protein from Arabidopsis Thaliana AT4G34215 at 1.6 Angstrom Resolution [Arabidopsis thaliana]
1DEO_A 8.11e-14 27 234 2 212
RHAMNOGALACTURONANACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.55 A RESOLUTION WITH SO4 IN THE ACTIVE SITE [Aspergillus aculeatus],1DEX_A RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.9 A RESOLUTION [Aspergillus aculeatus],1K7C_A Rhamnogalacturonan acetylesterase with seven N-linked carbohydrate residues distributed at two N-glycosylation sites refined at 1.12 A resolution [Aspergillus aculeatus],1PP4_A The crystal structure of rhamnogalacturonan acetylesterase in space group P3121 [Aspergillus aculeatus],1PP4_B The crystal structure of rhamnogalacturonan acetylesterase in space group P3121 [Aspergillus aculeatus]
3C1U_A 3.67e-13 27 234 2 212
ChainA, Rhamnogalacturonan acetylesterase [Aspergillus aculeatus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31523 3.77e-34 24 256 4 228
Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
O31528 1.05e-30 28 242 5 206
Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
Q8L9J9 1.21e-22 300 548 2 253
Probable carbohydrate esterase At4g34215 OS=Arabidopsis thaliana OX=3702 GN=At4g34215 PE=1 SV=2
Q5BAA2 3.99e-13 11 250 3 240
Rhamnogalacturonan acetylesterase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=AN2528 PE=1 SV=1
Q00017 5.82e-13 27 234 19 229
Rhamnogalacturonan acetylesterase OS=Aspergillus aculeatus OX=5053 GN=rha1 PE=1 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
0.503867 0.455238 0.040356 0.000167 0.000165 0.000198

TMHMM  Annotations      download full data without filtering help

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