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CAZyme Information: MGYG000001920_00980

You are here: Home > Sequence: MGYG000001920_00980

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 sp900546355
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900546355
CAZyme ID MGYG000001920_00980
CAZy Family GH115
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
855 97507.41 5.4326
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001920 3068459 MAG Denmark Europe
Gene Location Start: 18625;  End: 21192  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.131

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH115 32 833 3.4e-281 0.9956958393113343

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam15979 Glyco_hydro_115 0.0 182 530 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 1.59e-43 677 845 1 168
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 5.29e-10 45 149 24 120
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).
pfam05124 S_layer_C 0.001 85 151 153 219
S-layer like family, C-terminal region.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT26893.1 0.0 1 854 1 842
QDH54071.1 0.0 1 854 1 842
QUR44901.1 0.0 1 854 1 842
QUT78586.1 0.0 1 855 1 843
QDM11119.1 0.0 1 855 1 843

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 1 855 12 854
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 33 854 17 838
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
7PXQ_A 0.0 33 854 16 837
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
4ZMH_A 2.03e-171 44 851 25 934
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 1.86e-124 85 653 65 647
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
0.000638 0.990703 0.007954 0.000255 0.000210 0.000197

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001920_00980.