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CAZyme Information: MGYG000001376_01553

You are here: Home > Sequence: MGYG000001376_01553

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 Dysgonomonas gadei
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae; Dysgonomonas; Dysgonomonas gadei
CAZyme ID MGYG000001376_01553
CAZy Family GH11
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
898 MGYG000001376_3|CGC6 101059.7 6.247
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001376 5166013 Isolate not provided not provided
Gene Location Start: 231547;  End: 234243  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.8

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH11 674 863 8e-69 0.9830508474576272

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00457 Glyco_hydro_11 1.33e-71 673 862 1 175
Glycosyl hydrolases family 11.
pfam03629 SASA 1.60e-14 407 509 98 200
Carbohydrate esterase, sialic acid-specific acetylesterase. The catalytic triad of this esterase enzyme comprises residues Ser127, His403 and Asp391 in UniProtKB:P70665.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CCO21319.1 0.0 20 865 14 832
CCO21108.1 0.0 20 865 14 832
CCO21289.1 0.0 20 865 14 832
CCO21210.1 0.0 20 865 14 832
CCO21153.1 0.0 20 865 14 832

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7KMM_A 1.31e-124 30 635 25 631
ChainA, Sialic acid-specific 9-O-acetylesterase [Xanthomonas citri pv. citri str. 306],7KMM_B Chain B, Sialic acid-specific 9-O-acetylesterase [Xanthomonas citri pv. citri str. 306]
2F6B_A 5.25e-94 662 870 1 201
Structuraland active site modification studies implicate Glu, Trp and Arg in the activity of xylanase from alkalophilic Bacillus sp. (NCL 87-6-10). [Bacillus],2F6B_B Structural and active site modification studies implicate Glu, Trp and Arg in the activity of xylanase from alkalophilic Bacillus sp. (NCL 87-6-10). [Bacillus]
1H4G_A 2.92e-93 663 870 2 201
Oligosaccharide-bindingto family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre [Salipaludibacillus agaradhaerens],1H4G_B Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre [Salipaludibacillus agaradhaerens],1QH6_A CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE [Salipaludibacillus agaradhaerens],1QH6_B CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE [Salipaludibacillus agaradhaerens],1QH7_A CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE [Salipaludibacillus agaradhaerens],1QH7_B CATALYSIS AND SPECIFICITY IN ENZYMATIC GLYCOSIDE HYDROLASES: A 2,5B CONFORMATION FOR THE GLYCOSYL-ENZYME INTERMIDIATE REVEALED BY THE STRUCTURE OF THE BACILLUS AGARADHAERENS FAMILY 11 XYLANASE [Salipaludibacillus agaradhaerens]
1H4H_A 8.55e-93 663 877 2 208
Oligosaccharide-bindingto family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre [Salipaludibacillus agaradhaerens],1H4H_B Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre [Salipaludibacillus agaradhaerens],1H4H_C Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre [Salipaludibacillus agaradhaerens],1H4H_D Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre [Salipaludibacillus agaradhaerens]
6KKA_A 4.62e-90 664 871 2 201
XylanaseJ mutant from Bacillus sp. 41M-1 [Bacillus sp. 41M-1],6KKA_B Xylanase J mutant from Bacillus sp. 41M-1 [Bacillus sp. 41M-1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GJ44 2.26e-85 653 871 23 232
Endo-1,4-beta-xylanase A OS=Thermoclostridium stercorarium OX=1510 GN=xynA PE=1 SV=2
P17137 2.48e-85 658 871 57 260
Endo-1,4-beta-xylanase OS=Clostridium saccharobutylicum OX=169679 GN=xynB PE=3 SV=1
P83513 3.54e-83 661 878 16 223
Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A PE=1 SV=2
P33558 1.31e-82 653 871 23 233
Endo-1,4-beta-xylanase A OS=Thermoclostridium stercorarium OX=1510 GN=xynA PE=1 SV=2
P00694 7.03e-79 656 872 20 228
Endo-1,4-beta-xylanase A OS=Bacillus pumilus OX=1408 GN=xynA PE=1 SV=2

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
0.000448 0.998914 0.000168 0.000153 0.000144 0.000142

TMHMM  Annotations      download full data without filtering help

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