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CAZyme Information: MGYG000004561_01771

You are here: Home > Sequence: MGYG000004561_01771

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 sp002480935
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp002480935
CAZyme ID MGYG000004561_01771
CAZy Family CE12
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
413 47291.77 8.3084
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004561 3001921 MAG France Europe
Gene Location Start: 9969;  End: 11210  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004561_01771.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE12 162 366 1.3e-64 0.9857142857142858

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd01821 Rhamnogalacturan_acetylesterase_like 1.23e-75 161 365 1 195
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 1.32e-13 155 365 3 205
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
pfam13472 Lipase_GDSL_2 4.63e-10 176 316 16 152
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd00229 SGNH_hydrolase 1.13e-08 178 364 20 184
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.
cd01834 SGNH_hydrolase_like_2 3.20e-07 161 326 3 168
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
AGB29274.1 1.56e-197 2 413 9 419
BCS85052.1 2.30e-192 48 413 15 380
QIM09958.1 1.84e-177 33 413 17 400
ADE81025.1 7.14e-171 49 413 20 384
QVJ82311.1 1.11e-167 49 413 20 384

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2O14_A 1.07e-15 57 369 80 360
X-RayCrystal Structure of Protein YXIM_BACsu from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR595 [Bacillus subtilis]
1DEO_A 4.35e-06 162 236 2 75
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 4.35e-06 162 236 2 75
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 3.12e-45 163 380 8 224
Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
O31528 1.67e-23 160 382 2 216
Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
P42304 2.37e-16 57 369 95 375
Uncharacterized esterase YxiM OS=Bacillus subtilis (strain 168) OX=224308 GN=yxiM PE=1 SV=2
Q5BAA2 2.20e-08 148 236 5 87
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 8.05e-07 148 236 5 92
Rhamnogalacturonan acetylesterase OS=Aspergillus aculeatus OX=5053 GN=rha1 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
0.006389 0.992461 0.000283 0.000374 0.000244 0.000233

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004561_01771.