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CAZyme Information: MGYG000001537_01581

You are here: Home > Sequence: MGYG000001537_01581

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 Cellulomonas timonensis
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Cellulomonadaceae; Cellulomonas; Cellulomonas timonensis
CAZyme ID MGYG000001537_01581
CAZy Family CE4
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1196 MGYG000001537_11|CGC12 125390.57 4.2509
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001537 4057828 Isolate not provided not provided
Gene Location Start: 492163;  End: 495753  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.8

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH10 395 713 5e-97 0.9570957095709571
CBM9 890 1063 1.9e-44 0.9945054945054945
CBM22 230 360 1.5e-32 0.9618320610687023
CE4 28 148 2.8e-25 0.8769230769230769

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00331 Glyco_hydro_10 1.99e-105 396 713 11 310
Glycosyl hydrolase family 10.
smart00633 Glyco_10 9.81e-105 427 711 1 263
Glycosyl hydrolase family 10.
COG3693 XynA 1.23e-74 413 713 53 339
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism].
cd00005 CBM9_like_1 2.24e-68 887 1063 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.
pfam06452 CBM9_1 5.92e-49 890 1063 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
AEE44714.1 0.0 8 1166 195 1347
VEH27086.1 0.0 8 1166 195 1347
CAA90745.1 0.0 8 1166 33 1184
QHT58010.1 0.0 8 1168 195 1343
ARU50627.1 0.0 8 1071 158 1225

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3W24_A 4.71e-83 382 716 2 328
Thehigh-resolution crystal structure of TsXylA, intracellular xylanase from Thermoanaerobacterium saccharolyticum JW/SL-YS485 [Thermoanaerobacterium saccharolyticum JW/SL-YS485]
3W25_A 3.22e-82 382 716 2 328
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 3.22e-82 382 716 2 328
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]
6FHE_A 6.15e-73 383 712 7 339
Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct]
2DEP_A 6.77e-72 385 727 4 356
CrystalStructure of xylanase B from Clostridium stercorarium F9 [Thermoclostridium stercorarium],2DEP_B Crystal Structure of xylanase B from Clostridium stercorarium F9 [Thermoclostridium stercorarium]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P36917 4.34e-144 229 1059 198 1038
Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1
P38535 2.51e-142 229 1059 39 890
Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
Q60042 1.61e-118 214 1064 193 1054
Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1
O69230 2.08e-117 214 1064 190 1084
Endo-1,4-beta-xylanase C OS=Paenibacillus barcinonensis OX=198119 GN=xynC PE=1 SV=1
Q60037 1.47e-113 214 1064 198 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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000055 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001537_01581.