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CAZyme Information: MGYG000000695_01607

You are here: Home > Sequence: MGYG000000695_01607

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 sp000436035
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp000436035
CAZyme ID MGYG000000695_01607
CAZy Family GH115
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
838 95560.6 8.2812
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000695 3484843 MAG Kazakhstan Asia
Gene Location Start: 39451;  End: 41967  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.131

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH115 33 820 1.3e-278 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 0.0 182 514 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 1.95e-52 677 836 1 172
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 1.07e-06 26 149 5 120
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
QIU93956.1 0.0 1 838 1 821
QUT92919.1 0.0 19 837 23 828
ALJ61511.1 0.0 19 837 23 828
EDV05080.1 0.0 10 838 30 845
QDO71564.1 0.0 19 838 8 814

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4C90_A 3.48e-265 1 837 12 849
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 7.69e-258 34 837 17 834
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
7PXQ_A 5.48e-255 34 837 16 833
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
4ZMH_A 1.14e-202 23 833 5 929
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 1.07e-149 54 837 31 963
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
0.000271 0.999018 0.000185 0.000161 0.000162 0.000147

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000695_01607.