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CAZyme Information: MGYG000004471_01819

You are here: Home > Sequence: MGYG000004471_01819

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 UBA1394 sp900554975
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UBA1394; UBA1394 sp900554975
CAZyme ID MGYG000004471_01819
CAZy Family GH11
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
958 103544.58 4.34
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004471 1997651 MAG Israel Asia
Gene Location Start: 3487;  End: 6363  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.8 3.1.1.72

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH11 52 237 5.8e-73 0.9943502824858758
CE1 533 768 2.3e-35 0.9647577092511013
CBM22 264 391 8.1e-33 0.9694656488549618
CBM22 789 916 8.8e-31 0.9618320610687023

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00457 Glyco_hydro_11 1.25e-75 52 235 1 175
Glycosyl hydrolases family 11.
pfam02018 CBM_4_9 2.60e-23 261 395 1 134
Carbohydrate binding domain. This family includes diverse carbohydrate binding domains.
COG2382 Fes 1.05e-22 520 772 65 298
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism].
cd14256 Dockerin_I 6.72e-18 420 472 1 57
Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
pfam02018 CBM_4_9 2.82e-17 788 920 4 134
Carbohydrate binding domain. This family includes diverse carbohydrate binding domains.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CAB93667.1 2.07e-201 46 771 32 792
AAR39816.1 8.97e-193 40 742 28 782
CAA90271.1 8.97e-193 40 742 28 782
CBL18305.1 8.15e-192 6 958 7 668
CBL17231.1 1.43e-129 208 772 507 1074

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7AYL_A 7.23e-85 49 245 38 231
Crystalstructure of the GH11 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides [uncultured bacterium],7AYL_B Crystal structure of the GH11 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides [uncultured bacterium]
2F6B_A 7.02e-83 45 245 5 203
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 1.41e-82 45 245 5 203
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]
6KKA_A 1.92e-82 49 246 8 203
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]
1IGO_A 2.54e-82 49 246 10 203
Family11 xylanase [Bacillus subtilis],1IGO_B Family 11 xylanase [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q53317 2.29e-102 41 440 30 458
Xylanase/beta-glucanase OS=Ruminococcus flavefaciens OX=1265 GN=xynD PE=3 SV=2
P17137 1.71e-83 49 244 68 260
Endo-1,4-beta-xylanase OS=Clostridium saccharobutylicum OX=169679 GN=xynB PE=3 SV=1
Q8GJ44 8.11e-83 1 259 1 247
Endo-1,4-beta-xylanase A OS=Thermoclostridium stercorarium OX=1510 GN=xynA PE=1 SV=2
P33558 1.19e-79 1 259 1 248
Endo-1,4-beta-xylanase A OS=Thermoclostridium stercorarium OX=1510 GN=xynA PE=1 SV=2
P83513 2.27e-79 31 245 9 217
Bifunctional xylanase/deacetylase OS=Pseudobutyrivibrio xylanivorans OX=185007 GN=xyn11A 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
0.000236 0.999103 0.000203 0.000171 0.000156 0.000142

TMHMM  Annotations      download full data without filtering help

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