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CAZyme Information: MGYG000003200_00467

You are here: Home > Sequence: MGYG000003200_00467

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 CAG-873 sp900759845
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp900759845
CAZyme ID MGYG000003200_00467
CAZy Family CE12
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
325 36167.03 9.7428
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003200 2708478 MAG United States North America
Gene Location Start: 762;  End: 1739  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003200_00467.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE12 65 281 9.4e-54 0.9904761904761905

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd01821 Rhamnogalacturan_acetylesterase_like 8.72e-71 63 281 1 198
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.
cd00229 SGNH_hydrolase 2.02e-11 64 271 1 178
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 2.32e-10 67 271 1 175
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
COG2755 TesA 1.14e-09 63 282 9 209
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd01834 SGNH_hydrolase_like_2 4.15e-08 60 271 1 182
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
QIU94558.1 9.19e-162 9 311 13 315
ADY37518.1 8.22e-161 18 311 18 314
ALA72204.1 1.17e-160 10 311 11 314
AND18183.1 1.17e-160 10 311 11 314
AII64734.1 1.17e-160 10 311 11 314

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1DEO_A 7.51e-31 65 281 3 212
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 4.00e-30 65 281 3 212
ChainA, Rhamnogalacturonan acetylesterase [Aspergillus aculeatus]
2O14_A 1.46e-12 62 282 162 360
X-RayCrystal Structure of Protein YXIM_BACsu from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR595 [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q00017 6.17e-30 65 281 20 229
Rhamnogalacturonan acetylesterase OS=Aspergillus aculeatus OX=5053 GN=rha1 PE=1 SV=1
Q5BAA2 7.67e-30 65 299 20 241
Rhamnogalacturonan acetylesterase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=AN2528 PE=1 SV=1
O31528 3.26e-20 65 294 5 214
Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
P42304 3.15e-13 62 282 177 375
Uncharacterized esterase YxiM OS=Bacillus subtilis (strain 168) OX=224308 GN=yxiM PE=1 SV=2

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
0.000347 0.998865 0.000199 0.000215 0.000191 0.000167

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003200_00467.