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CAZyme Information: MGYG000004763_00633

You are here: Home > Sequence: MGYG000004763_00633

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-462 sp900291465
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; CAG-462; CAG-462 sp900291465
CAZyme ID MGYG000004763_00633
CAZy Family CE12
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
549 MGYG000004763_4|CGC3 61880.92 9.4474
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004763 3504022 MAG Denmark Europe
Gene Location Start: 120429;  End: 122078  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004763_00633.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE12 318 537 1e-62 0.9904761904761905
CE12 67 286 1e-52 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 4.14e-79 316 537 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.
cd01821 Rhamnogalacturan_acetylesterase_like 3.13e-74 65 286 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 6.90e-15 67 277 1 179
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 9.00e-13 65 288 9 210
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
COG2755 TesA 7.55e-12 315 541 8 212
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
QEW35578.1 0.0 10 549 8 547
QQY43084.1 0.0 10 549 8 547
ABR37888.1 0.0 10 549 8 547
QQY39782.1 0.0 10 549 8 547
QUT56845.1 0.0 10 549 8 547

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1DEO_A 3.49e-30 318 548 3 223
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 1.70e-29 318 548 3 223
ChainA, Rhamnogalacturonan acetylesterase [Aspergillus aculeatus]
2O14_A 2.83e-14 318 541 165 363
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
Q5BAA2 2.46e-33 318 548 20 235
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 2.89e-29 318 548 20 240
Rhamnogalacturonan acetylesterase OS=Aspergillus aculeatus OX=5053 GN=rha1 PE=1 SV=1
O31523 1.14e-27 318 548 8 223
Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
O31528 6.23e-23 318 548 5 213
Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
P42304 1.20e-14 318 541 180 378
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
0.016461 0.982047 0.000403 0.000390 0.000309 0.000359

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004763_00633.