logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001222_00320

You are here: Home > Sequence: MGYG000001222_00320

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 UMGS1326 sp900550775
Lineage Bacteria; Firmicutes_A; Clostridia; Monoglobales; Monoglobaceae; UMGS1326; UMGS1326 sp900550775
CAZyme ID MGYG000001222_00320
CAZy Family CE12
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1625 178067.76 4.6591
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001222 2203618 MAG Austria Europe
Gene Location Start: 23245;  End: 28122  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001222_00320.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE12 1400 1611 1e-52 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 3.91e-60 1399 1611 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.
cd10967 CE4_GLA_like_6s 2.54e-22 1110 1310 1 186
Putative catalytic NodB homology domain of gellan lyase and similar proteins. This family is represented by the extracellular polysaccharide-degrading enzyme, gellan lyase (gellanase, EC 4.2.2.-), from Bacillus sp. The enzyme acts on gellan exolytically and releases a tetrasaccharide of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the nonreducing terminus. The family also includes many uncharacterized prokaryotic polysaccharide deacetylases, which show high sequence similarity to Bacillus sp. gellan lyase. Although their biological functions remain unknown, all members of the family contain a conserved domain with a 6-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.
COG2755 TesA 9.32e-18 1397 1613 7 210
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd00229 SGNH_hydrolase 1.32e-09 1401 1609 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 2.35e-09 1405 1602 3 176
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SQI59078.1 2.25e-38 1401 1611 6 204
QYR23667.1 1.09e-36 1395 1625 4 220
QUW24061.1 1.32e-36 1395 1625 1 216
QNF28850.1 1.54e-35 1392 1615 33 254
AOV08603.1 1.60e-35 1395 1611 1 205

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1DEO_A 3.66e-11 1400 1611 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 1.64e-10 1400 1611 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
O31528 2.44e-32 1401 1612 5 203
Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
O31523 3.20e-27 1401 1612 8 213
Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
Q00017 2.60e-10 1400 1611 19 229
Rhamnogalacturonan acetylesterase OS=Aspergillus aculeatus OX=5053 GN=rha1 PE=1 SV=1
Q5BAA2 3.53e-09 1400 1611 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

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
0.000244 0.999059 0.000168 0.000190 0.000164 0.000144

TMHMM  Annotations      download full data without filtering help

start end
12 34