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CAZyme Information: MGYG000000902_00304

You are here: Home > Sequence: MGYG000000902_00304

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 neonatale
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium neonatale
CAZyme ID MGYG000000902_00304
CAZy Family CBM22
CAZyme Description Endo-1,4-beta-xylanase C
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
913 MGYG000000902_2|CGC3 102534.19 4.5455
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000902 4770522 MAG China Asia
Gene Location Start: 107905;  End: 110646  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 213 555 3.2e-105 0.9900990099009901
CBM9 740 911 1.3e-47 0.9945054945054945
CBM22 46 173 1.3e-30 0.9618320610687023
CBM9 576 721 1.3e-20 0.967032967032967

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00331 Glyco_hydro_10 3.00e-122 213 555 1 310
Glycosyl hydrolase family 10.
smart00633 Glyco_10 1.08e-112 255 553 1 263
Glycosyl hydrolase family 10.
COG3693 XynA 6.60e-101 233 554 46 338
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism].
cd00005 CBM9_like_1 2.32e-75 730 912 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.
pfam06452 CBM9_1 4.83e-42 740 912 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
BCZ47833.1 4.44e-299 193 912 40 758
QKS59245.1 1.23e-237 46 912 201 1084
CAA07173.1 3.47e-237 53 912 209 1084
QOS77886.1 9.28e-232 36 912 28 940
APO44853.1 5.52e-230 43 911 41 937

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4W8L_A 1.13e-132 209 563 1 351
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 7.58e-101 205 554 5 339
Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct]
3W24_A 5.45e-99 207 558 3 328
Thehigh-resolution crystal structure of TsXylA, intracellular xylanase from Thermoanaerobacterium saccharolyticum JW/SL-YS485 [Thermoanaerobacterium saccharolyticum JW/SL-YS485]
3W27_A 4.10e-98 207 558 3 328
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]
3W25_A 4.10e-98 207 558 3 328
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O69230 6.94e-238 53 912 209 1084
Endo-1,4-beta-xylanase C OS=Paenibacillus barcinonensis OX=198119 GN=xynC PE=1 SV=1
P36917 6.45e-216 40 913 193 1044
Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1
P38535 2.30e-210 39 913 34 896
Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
Q60037 1.84e-156 32 912 193 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 5.07e-149 44 912 200 1054
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
0.012410 0.980309 0.006281 0.000446 0.000270 0.000253

TMHMM  Annotations      download full data without filtering help

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