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CAZyme Information: MGYG000002478_00033

You are here: Home > Sequence: MGYG000002478_00033

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 dorei
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola dorei
CAZyme ID MGYG000002478_00033
CAZy Family GH115
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
864 MGYG000002478_1|CGC2 99442.32 6.1352
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002478 5444912 Isolate Finland Europe
Gene Location Start: 37586;  End: 40180  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.131

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH115 36 837 8.3e-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 0.0 186 534 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 3.43e-36 682 853 2 172
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 3.64e-04 56 153 31 120
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
QJR60928.1 0.0 1 864 1 864
ALA72079.1 0.0 1 864 1 864
QJR54274.1 0.0 1 864 1 864
AII66220.1 0.0 1 864 1 864
QUT85336.1 0.0 1 864 1 864

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 9 858 15 853
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 23 861 3 841
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
7PXQ_A 0.0 23 858 2 837
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
4ZMH_A 1.47e-170 48 670 25 633
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 2.05e-118 86 658 62 648
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
0.000430 0.997606 0.001384 0.000183 0.000174 0.000171

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002478_00033.