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CAZyme Information: MGYG000001789_01680

You are here: Home > Sequence: MGYG000001789_01680

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 Phocaeicola sp002161565
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp002161565
CAZyme ID MGYG000001789_01680
CAZy Family CE12
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
430 MGYG000001789_25|CGC1 48525.93 6.6154
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001789 3544186 MAG Denmark Europe
Gene Location Start: 13831;  End: 15123  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001789_01680.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE12 181 386 9.9e-69 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 3.20e-89 180 386 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 2.38e-14 174 387 3 209
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
pfam13472 Lipase_GDSL_2 3.00e-08 186 378 3 176
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd00229 SGNH_hydrolase 1.64e-05 182 384 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.
cd01834 SGNH_hydrolase_like_2 0.002 245 385 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
ADY37533.1 6.17e-235 19 430 928 1339
ALK86443.1 1.75e-216 11 430 5 424
QQY43066.1 1.75e-216 11 430 5 424
QQY39765.1 1.75e-216 11 430 5 424
ABR37910.1 1.75e-216 11 430 5 424

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2O14_A 1.05e-17 76 387 80 360
X-RayCrystal Structure of Protein YXIM_BACsu from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR595 [Bacillus subtilis]
1DEO_A 9.15e-09 181 386 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 4.05e-08 181 386 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 1.28e-53 182 400 8 222
Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
O31528 3.30e-27 182 397 5 213
Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
P42304 3.09e-18 76 387 95 375
Uncharacterized esterase YxiM OS=Bacillus subtilis (strain 168) OX=224308 GN=yxiM PE=1 SV=2
Q5BAA2 1.61e-09 181 386 19 224
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 6.01e-08 181 386 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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000428 0.998811 0.000210 0.000185 0.000171 0.000163

TMHMM  Annotations      download full data without filtering help

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