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CAZyme Information: MGYG000001129_01099

You are here: Home > Sequence: MGYG000001129_01099

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 Ruminococcus_C sp000437255
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp000437255
CAZyme ID MGYG000001129_01099
CAZy Family CBM22
CAZyme Description Endo-1,4-beta-xylanase A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1148 MGYG000001129_152|CGC1 126067.57 4.1996
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001129 1878365 MAG China Asia
Gene Location Start: 9996;  End: 13442  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 351 693 5.8e-94 0.9933993399339934
CBM9 874 1047 1.7e-47 0.9945054945054945
CBM22 36 159 1.1e-31 0.9541984732824428
CBM22 188 316 5e-29 0.9618320610687023

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00331 Glyco_hydro_10 1.07e-101 352 693 1 310
Glycosyl hydrolase family 10.
smart00633 Glyco_10 2.74e-89 418 691 12 263
Glycosyl hydrolase family 10.
cd00005 CBM9_like_1 5.98e-77 862 1048 1 185
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 2.19e-68 357 693 31 339
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism].
pfam06452 CBM9_1 6.91e-54 874 1048 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 1.68e-193 4 1052 6 1047
QEH67940.1 3.30e-193 4 1052 8 1049
BAA21516.2 2.06e-159 191 694 39 544
ANV77297.1 2.06e-159 191 694 39 544
ABN53059.1 2.06e-159 191 694 39 544

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2W5F_A 1.16e-94 216 691 54 524
ChainA, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus],2W5F_B Chain B, ENDO-1,4-BETA-XYLANASE Y [Acetivibrio thermocellus]
2WYS_A 7.67e-92 216 691 54 524
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]
3W24_A 1.15e-56 344 703 1 335
Thehigh-resolution crystal structure of TsXylA, intracellular xylanase from Thermoanaerobacterium saccharolyticum JW/SL-YS485 [Thermoanaerobacterium saccharolyticum JW/SL-YS485]
3W27_A 7.35e-56 344 703 1 335
Thehigh-resolution crystal structure of TsXylA, intracellular xylanase from /Thermoanaerobacterium saccharolyticum JW/SL-YS485/: the complex of the E251A mutant with xylobiose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3W28_A The high-resolution crystal structure of TsXylA, intracellular xylanase from /Thermoanaerobacterium saccharolyticum JW/SL-YS485/: the complex of the E251A mutant with xylotriose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3W29_A The high-resolution crystal structure of TsXylA, intracellular xylanase from /Thermoanaerobacterium saccharolyticum JW/SL-YS485/: the complex of the E251A mutant with xylotetraose [Thermoanaerobacterium saccharolyticum JW/SL-YS485]
3W25_A 7.35e-56 344 703 1 335
Thehigh-resolution crystal structure of TsXylA, intracellular xylanase from /Thermoanaerobacterium saccharolyticum JW/SL-YS485/: the complex of the E146A mutant with xylobiose [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3W26_A The high-resolution crystal structure of TsXylA, intracellular xylanase from /Thermoanaerobacterium saccharolyticum JW/SL-YS485/: the complex of the E146A mutant with xylotriose [Thermoanaerobacterium saccharolyticum JW/SL-YS485]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P36917 4.37e-135 39 1049 46 1044
Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1
Q60037 1.08e-127 9 1048 29 1058
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 9.89e-126 53 1048 68 1054
Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1
O69230 5.01e-124 2 1048 4 1084
Endo-1,4-beta-xylanase C OS=Paenibacillus barcinonensis OX=198119 GN=xynC PE=1 SV=1
P38535 2.72e-112 191 1055 44 902
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
0.000825 0.758653 0.239291 0.000498 0.000400 0.000302

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001129_01099.