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CAZyme Information: MGYG000000964_01932

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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 salanitronis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola salanitronis
CAZyme ID MGYG000000964_01932
CAZy Family GH106
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1339 MGYG000000964_47|CGC1 151385.89 5.8001
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000964 3100012 MAG Denmark Europe
Gene Location Start: 8570;  End: 12589  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000964_01932.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH106 19 918 2.4e-303 0.9951456310679612
CE12 1089 1293 4.4e-68 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 1.95e-82 1088 1294 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.
pfam17132 Glyco_hydro_106 7.65e-58 174 708 354 865
COG2755 TesA 1.06e-11 1082 1297 3 211
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
pfam13472 Lipase_GDSL_2 2.30e-08 1094 1286 3 176
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd00229 SGNH_hydrolase 2.61e-05 1090 1292 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADY37533.1 0.0 1 1339 1 1339
QUT27363.1 0.0 2 934 3 930
QDH54512.1 0.0 2 925 3 921
QQR18621.1 0.0 2 925 3 921
ANU56532.1 0.0 2 925 3 921

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6Q2F_A 1.07e-40 174 918 413 1139
Structureof Rhamnosidase from Novosphingobium sp. PP1Y [Novosphingobium sp. PP1Y]
5MQM_A 4.64e-39 69 877 275 1065
Glycosidehydrolase BT_0986 [Bacteroides thetaiotaomicron],5MQN_A Glycoside hydrolase BT_0986 [Bacteroides thetaiotaomicron]
5MWK_A 1.06e-38 69 877 275 1065
Glycosidehydrolase BT_0986 [Bacteroides thetaiotaomicron]
2O14_A 2.28e-17 937 1296 16 361
X-RayCrystal Structure of Protein YXIM_BACsu from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR595 [Bacillus subtilis]
1DEO_A 7.36e-07 1089 1294 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31523 8.39e-52 1090 1305 8 223
Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
O31528 3.74e-28 1090 1303 5 211
Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
P42304 2.26e-18 937 1296 31 376
Uncharacterized esterase YxiM OS=Bacillus subtilis (strain 168) OX=224308 GN=yxiM PE=1 SV=2
T2KNA8 4.94e-10 701 873 921 1095
Putative beta-glucuronidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22040 PE=2 SV=1
Q00017 4.84e-06 1089 1294 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

0.000368 0.998801 0.000253 0.000203 0.000181 0.000171

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000964_01932.