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CAZyme Information: MGYG000001756_00968

You are here: Home > Sequence: MGYG000001756_00968

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 sp900538575
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UBA1394; UBA1394 sp900538575
CAZyme ID MGYG000001756_00968
CAZy Family CBM22
CAZyme Description Endo-1,4-beta-xylanase A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1095 122329.01 4.2994
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001756 2438245 MAG Iceland Europe
Gene Location Start: 647;  End: 3934  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.8 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH10 353 694 2.1e-89 0.9933993399339934
CBM9 857 1030 2.5e-48 0.9945054945054945
CBM22 34 162 2e-36 0.9770992366412213
CBM22 190 316 9e-29 0.9541984732824428

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00331 Glyco_hydro_10 1.65e-98 354 694 1 310
Glycosyl hydrolase family 10.
smart00633 Glyco_10 9.16e-95 395 692 1 263
Glycosyl hydrolase family 10.
cd00005 CBM9_like_1 6.49e-80 854 1030 8 184
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.
COG3693 XynA 1.70e-64 383 694 55 339
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism].
pfam06452 CBM9_1 4.72e-56 857 1031 1 182
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
ADZ82256.1 1.81e-210 1 1030 3 1042
QEH67940.1 5.37e-209 1 1030 5 1044
BAA21516.2 2.20e-159 191 695 38 544
ANV77297.1 2.20e-159 191 695 38 544
ABN53059.1 2.20e-159 191 695 38 544

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2W5F_A 8.04e-99 191 693 28 525
ChainA, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2W5F_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus]
2WYS_A 1.53e-95 191 693 28 525
ChainA, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2WYS_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2WZE_A Chain A, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2WZE_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus]
5Y3X_A 1.54e-57 351 692 29 354
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]
7NL2_A 7.49e-56 343 708 2 350
ChainA, Beta-xylanase [Pseudothermotoga thermarum DSM 5069],7NL2_B Chain B, Beta-xylanase [Pseudothermotoga thermarum DSM 5069]
6FHE_A 1.81e-55 348 692 7 338
Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P36917 9.01e-141 25 1035 32 1047
Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1
Q60037 1.46e-140 51 1030 70 1057
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
O69230 1.13e-134 34 1030 38 1083
Endo-1,4-beta-xylanase C OS=Paenibacillus barcinonensis OX=198119 GN=xynC PE=1 SV=1
Q60042 1.57e-133 51 1030 65 1053
Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1
P38535 4.77e-110 192 1035 44 899
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
0.000241 0.999052 0.000210 0.000190 0.000146 0.000134

TMHMM  Annotations      download full data without filtering help

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7 29