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CAZyme Information: MGYG000002835_01686

You are here: Home > Sequence: MGYG000002835_01686

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 Fusicatenibacter sp900543115
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Fusicatenibacter; Fusicatenibacter sp900543115
CAZyme ID MGYG000002835_01686
CAZy Family CBM22
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1055 MGYG000002835_33|CGC1 116442.91 3.9762
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002835 2863124 MAG United States North America
Gene Location Start: 18269;  End: 21436  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.8

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH10 376 689 7.5e-106 0.9900990099009901
CBM9 717 887 2.9e-48 0.9835164835164835
CBM22 37 165 9.2e-26 0.9694656488549618
CBM22 211 321 7.5e-21 0.8549618320610687

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00331 Glyco_hydro_10 9.34e-111 376 689 1 310
Glycosyl hydrolase family 10.
smart00633 Glyco_10 2.41e-100 416 687 1 263
Glycosyl hydrolase family 10.
COG3693 XynA 2.05e-81 406 698 57 345
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism].
cd00005 CBM9_like_1 6.49e-78 710 887 4 182
DOMON-like type 9 carbohydrate binding module of xylanases. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.
pfam06452 CBM9_1 2.27e-54 717 888 1 180
Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AFH63098.1 1.14e-173 71 895 297 1124
QGH36727.1 2.16e-173 71 900 305 1137
AEI43097.1 9.92e-173 71 892 297 1120
AWP30060.1 4.34e-172 71 894 73 901
ASA19867.1 8.84e-172 73 902 77 912

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3RDK_A 1.10e-90 373 690 4 338
Proteincrystal structure of xylanase A1 of Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RDK_B Protein crystal structure of xylanase A1 of Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_A Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_B Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_C Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_D Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_E Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_F Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_G Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_H Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],4E4P_A Second native structure of Xylanase A1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],4E4P_B Second native structure of Xylanase A1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2]
6FHE_A 5.20e-75 368 688 5 339
Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct]
5OFJ_A 1.37e-74 366 689 1 337
Crystalstructure of N-terminal domain of bifunctional CbXyn10C [Caldicellulosiruptor bescii DSM 6725]
5OFK_A 9.40e-74 366 689 1 337
Crystalstructure of CbXyn10C variant E140Q/E248Q complexed with xyloheptaose [Caldicellulosiruptor bescii DSM 6725],5OFL_A Crystal structure of CbXyn10C variant E140Q/E248Q complexed with cellohexaose [Caldicellulosiruptor bescii DSM 6725]
5Y3X_A 1.62e-73 370 689 26 356
Crystalstructure of endo-1,4-beta-xylanase from Caldicellulosiruptor owensensis [Caldicellulosiruptor owensensis OL],5Y3X_B Crystal structure of endo-1,4-beta-xylanase from Caldicellulosiruptor owensensis [Caldicellulosiruptor owensensis OL],5Y3X_C Crystal structure of endo-1,4-beta-xylanase from Caldicellulosiruptor owensensis [Caldicellulosiruptor owensensis OL],5Y3X_D Crystal structure of endo-1,4-beta-xylanase from Caldicellulosiruptor owensensis [Caldicellulosiruptor owensensis OL],5Y3X_E Crystal structure of endo-1,4-beta-xylanase from Caldicellulosiruptor owensensis [Caldicellulosiruptor owensensis OL],5Y3X_F Crystal structure of endo-1,4-beta-xylanase from Caldicellulosiruptor owensensis [Caldicellulosiruptor owensensis OL]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
C6CRV0 5.98e-169 71 895 224 1055
Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
Q60037 4.06e-125 30 887 47 1055
Endo-1,4-beta-xylanase A OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=xynA PE=1 SV=1
Q60042 1.01e-122 12 887 19 1051
Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1
P36917 1.81e-116 13 897 16 1050
Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1
P38535 8.72e-104 213 895 45 900
Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1

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
0.001614 0.997443 0.000307 0.000236 0.000199 0.000185

TMHMM  Annotations      download full data without filtering help

start end
7 29
1033 1052