logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002962_00129

You are here: Home > Sequence: MGYG000002962_00129

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 Clostridium sp900543325
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900543325
CAZyme ID MGYG000002962_00129
CAZy Family CBM22
CAZyme Description Endo-1,4-beta-xylanase C
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1221 MGYG000002962_2|CGC2 137297.14 4.1803
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002962 3186188 MAG China Asia
Gene Location Start: 41038;  End: 44703  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.8

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH10 399 741 1.4e-103 0.976897689768977
CBM9 912 1082 2.1e-44 0.989010989010989
CBM22 221 347 5.5e-31 0.9465648854961832

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00331 Glyco_hydro_10 1.90e-112 405 741 12 310
Glycosyl hydrolase family 10.
smart00633 Glyco_10 5.42e-101 437 739 1 263
Glycosyl hydrolase family 10.
COG3693 XynA 1.28e-86 418 741 48 339
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism].
cd00005 CBM9_like_1 1.86e-77 902 1081 1 182
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 5.29e-46 912 1083 1 181
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
CAA07173.1 1.29e-226 25 1085 31 1085
QKS59245.1 1.82e-226 25 1085 31 1085
APO44853.1 1.52e-210 233 1085 59 939
BAA34091.1 6.15e-210 233 1085 60 940
QOS77886.1 7.61e-208 205 1083 34 939

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4W8L_A 1.00e-123 395 747 5 349
Structureof GH10 from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4W8L_B Structure of GH10 from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4W8L_C Structure of GH10 from Paenibacillus barcinonensis [Paenibacillus barcinonensis]
6FHE_A 1.85e-84 403 740 21 339
Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct]
3W24_A 3.07e-79 403 741 17 325
Thehigh-resolution crystal structure of TsXylA, intracellular xylanase from Thermoanaerobacterium saccharolyticum JW/SL-YS485 [Thermoanaerobacterium saccharolyticum JW/SL-YS485]
3W25_A 2.06e-78 403 741 17 325
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]
3W27_A 2.06e-78 403 741 17 325
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O69230 2.58e-227 25 1085 31 1085
Endo-1,4-beta-xylanase C OS=Paenibacillus barcinonensis OX=198119 GN=xynC PE=1 SV=1
P36917 1.97e-197 39 1084 45 1043
Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1
P38535 6.41e-176 235 1084 58 895
Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
Q60037 2.16e-144 56 1085 71 1059
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 8.04e-139 25 1085 37 1055
Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 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
0.000300 0.998972 0.000198 0.000197 0.000164 0.000149

TMHMM  Annotations      download full data without filtering help

start end
1197 1214