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CAZyme Information: MGYG000000013_01935

You are here: Home > Sequence: MGYG000000013_01935

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 Bacteroides sp902362375
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp902362375
CAZyme ID MGYG000000013_01935
CAZy Family GH105
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
713 MGYG000000013_4|CGC5 80841.32 7.3005
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000013 6368149 Isolate United Kingdom Europe
Gene Location Start: 413212;  End: 415353  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000013_01935.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH105 102 430 1.2e-76 0.9487951807228916
CE12 484 699 2.5e-54 0.9904761904761905

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07470 Glyco_hydro_88 2.02e-75 102 430 30 340
Glycosyl Hydrolase Family 88. Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases.
cd01821 Rhamnogalacturan_acetylesterase_like 3.50e-60 482 699 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.
COG4225 YesR 3.60e-37 100 412 33 332
Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism].
COG2755 TesA 6.06e-15 480 700 7 209
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd00229 SGNH_hydrolase 1.08e-10 484 697 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
VTZ55484.1 0.0 1 712 1 716
QMI82192.1 0.0 1 711 1 715
BBK85841.1 0.0 1 711 2 716
SCD19753.1 5.23e-284 43 711 48 713
QIK54909.1 1.56e-278 43 711 47 713

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3K11_A 4.64e-176 43 460 24 441
Crystalstructure of Putative glycosyl hydrolase (NP_813087.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.80 A resolution [Bacteroides thetaiotaomicron VPI-5482]
1DEO_A 1.03e-27 484 699 3 212
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 4.79e-27 484 699 3 212
ChainA, Rhamnogalacturonan acetylesterase [Aspergillus aculeatus]
1NC5_A 3.55e-20 202 434 124 369
Structureof Protein of Unknown Function of YteR from Bacillus Subtilis [Bacillus subtilis],2D8L_A Crystal Structure of Unsaturated Rhamnogalacturonyl Hydrolase in complex with dGlcA-GalNAc [Bacillus subtilis]
2GH4_A 5.67e-20 202 434 114 359
ChainA, Putative glycosyl hydrolase yteR [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q00017 3.37e-27 481 699 17 229
Rhamnogalacturonan acetylesterase OS=Aspergillus aculeatus OX=5053 GN=rha1 PE=1 SV=1
Q5BAA2 6.37e-24 481 699 17 224
Rhamnogalacturonan acetylesterase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=AN2528 PE=1 SV=1
O34559 1.94e-19 202 434 124 369
Unsaturated rhamnogalacturonyl hydrolase YteR OS=Bacillus subtilis (strain 168) OX=224308 GN=yteR PE=1 SV=1
O31521 8.46e-18 177 435 87 341
Unsaturated rhamnogalacturonyl hydrolase YesR OS=Bacillus subtilis (strain 168) OX=224308 GN=yesR PE=1 SV=1
O31528 2.73e-17 484 712 5 215
Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY 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
0.000186 0.999207 0.000154 0.000155 0.000144 0.000140

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000013_01935.