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CAZyme Information: MGYG000001237_00514

You are here: Home > Sequence: MGYG000001237_00514

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 UMGS1600 sp900553295
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; UMGS1600; UMGS1600 sp900553295
CAZyme ID MGYG000001237_00514
CAZy Family CE12
CAZyme Description Rhamnogalacturonan acetylesterase RhgT
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
234 MGYG000001237_14|CGC1 26316.76 5.7015
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001237 2708995 MAG Austria Europe
Gene Location Start: 7634;  End: 8338  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001237_00514.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE12 3 211 4.1e-72 0.9952380952380953

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd01821 Rhamnogalacturan_acetylesterase_like 3.37e-85 2 211 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.
COG2755 TesA 5.80e-22 3 219 10 216
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd00229 SGNH_hydrolase 1.52e-08 4 209 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.
pfam13472 Lipase_GDSL_2 2.16e-08 8 155 3 147
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd01834 SGNH_hydrolase_like_2 7.47e-07 70 210 63 191
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
CBL09365.1 8.81e-79 1 222 1 224
CBL11990.1 8.81e-79 1 222 1 224
VCV21969.1 1.02e-77 1 222 1 224
QNM03334.1 6.22e-77 1 225 1 227
QOV20143.1 6.69e-72 4 224 6 228

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2O14_A 1.37e-14 3 215 164 363
X-RayCrystal Structure of Protein YXIM_BACsu from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR595 [Bacillus subtilis]
1DEO_A 1.43e-10 2 200 1 201
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 6.85e-10 2 200 1 201
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 2.61e-54 4 215 8 216
Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
O31528 1.14e-40 4 215 5 206
Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
P42304 1.66e-14 3 215 179 378
Uncharacterized esterase YxiM OS=Bacillus subtilis (strain 168) OX=224308 GN=yxiM PE=1 SV=2
Q5BAA2 2.04e-11 3 204 19 217
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 9.28e-10 2 200 18 218
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
1.000067 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001237_00514.