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CAZyme Information: MGYG000000863_01259

You are here: Home > Sequence: MGYG000000863_01259

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 UMGS1490 sp900547395
Lineage Bacteria; Verrucomicrobiota; Verrucomicrobiae; Opitutales; CAG-312; UMGS1490; UMGS1490 sp900547395
CAZyme ID MGYG000000863_01259
CAZy Family GH115
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
850 MGYG000000863_14|CGC1 96669.23 8.4904
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000863 2015892 MAG United States North America
Gene Location Start: 17608;  End: 20160  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000863_01259.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH115 28 832 2.5e-228 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 1.77e-169 181 521 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 1.58e-24 687 847 7 170
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 0.002 78 146 48 118
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
EDV07546.1 7.64e-302 19 848 20 961
ALK86808.1 6.73e-298 1 848 2 962
AYD49386.1 5.78e-267 15 848 20 961
APZ45930.1 3.16e-265 6 849 11 956
AUC19792.1 3.16e-265 6 849 11 956

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5BY3_A 5.73e-162 32 835 21 773
Anovel family GH115 4-O-Methyl-alpha-glucuronidase, BtGH115A, with specificity for decorated arabinogalactans [Bacteroides thetaiotaomicron VPI-5482]
4C90_A 4.53e-136 2 845 12 844
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]
4ZMH_A 8.70e-115 22 644 6 607
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]
7PUG_A 1.89e-105 30 843 17 827
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
7PXQ_A 3.60e-105 30 843 16 826
ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]

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
0.000272 0.999107 0.000172 0.000146 0.000143 0.000137

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000863_01259.