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CAZyme Information: MGYG000002960_00224

You are here: Home > Sequence: MGYG000002960_00224

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 Prevotella sp900555035
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900555035
CAZyme ID MGYG000002960_00224
CAZy Family GH115
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
852 96772.22 8.1767
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002960 3004760 MAG China Asia
Gene Location Start: 60303;  End: 62861  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.131

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH115 37 838 7.8e-271 0.9913916786226685

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam15979 Glyco_hydro_115 0.0 185 521 1 334
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 4.10e-31 667 841 4 159
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 6.54e-05 72 152 43 120
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
QNT66545.1 0.0 1 852 1 852
BCS85271.1 0.0 1 841 1 814
CCG34758.1 0.0 36 841 1 784
QVJ82146.1 0.0 22 841 23 808
ADE81569.1 0.0 22 841 24 809

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4C90_A 0.0 7 841 13 835
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 0.0 37 841 19 820
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
7PXQ_A 0.0 37 841 18 819
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
4ZMH_A 3.12e-180 28 644 5 622
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]
6NPS_A 7.55e-120 47 649 23 652
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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000727 0.998339 0.000384 0.000214 0.000167 0.000156

TMHMM  Annotations      download full data without filtering help

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