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CAZyme Information: MGYG000003277_02967

You are here: Home > Sequence: MGYG000003277_02967

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 Duncaniella sp900762315
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Duncaniella; Duncaniella sp900762315
CAZyme ID MGYG000003277_02967
CAZy Family GH115
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
815 92822.91 5.155
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003277 3767547 MAG United States North America
Gene Location Start: 45263;  End: 47710  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.131

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH115 4 793 3.6e-226 0.9870875179340028

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam15979 Glyco_hydro_115 0.0 145 481 1 333
Glycosyl hydrolase family 115. Glyco_hydro_115 is a family of glycoside hydrolases likely to have the activity of xylan a-1,2-glucuronidase, EC:3.2.1.131, or a-(4-O-methyl)-glucuronidase EC:3.2.1.-.
pfam17829 GH115_C 2.40e-19 619 805 11 168
Gylcosyl hydrolase family 115 C-terminal domain. This domain is found at the C-terminus of glycosyl hydrolase family 115 proteins. This domain has a beta-sandwich fold.
pfam03648 Glyco_hydro_67N 1.59e-05 31 112 44 120
Glycosyl hydrolase family 67 N-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the N-terminal region of alpha-glucuronidase. The N-terminal domain forms a two-layer sandwich, each layer being formed by a beta sheet of five strands. A further two helices form part of the interface with the central, catalytic, module (pfam07488).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
EEC55419.1 0.0 10 804 55 985
QRQ50360.1 0.0 10 804 30 960
QUT25621.1 2.23e-289 5 804 50 1001
QRQ59056.1 4.87e-289 5 804 21 972
ALJ47135.1 1.11e-288 5 804 46 997

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZMH_A 1.08e-172 10 598 25 630
Crystalstructure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40],4ZMH_B Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40]
4C90_A 1.19e-168 8 809 54 843
Evidencethat GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C90_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_A Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus]
7PUG_A 2.33e-164 7 812 26 832
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
7PXQ_A 2.15e-161 7 812 25 831
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
6NPS_A 4.10e-134 1 598 13 654
Crystalstructure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112],6NPS_B Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112]

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000076 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003277_02967.