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CAZyme Information: MGYG000003402_03405

You are here: Home > Sequence: MGYG000003402_03405

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 Paenibacillus lactis
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus lactis
CAZyme ID MGYG000003402_03405
CAZy Family GH10
CAZyme Description Endo-1,4-beta-xylanase A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
953 MGYG000003402_1160|CGC1 102974.8 5.1607
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003402 5924245 MAG United States North America
Gene Location Start: 3829;  End: 6690  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 4 309 3.1e-98 0.900990099009901
CBM9 336 508 1.7e-56 0.9945054945054945

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00331 Glyco_hydro_10 1.16e-111 2 309 27 310
Glycosyl hydrolase family 10.
smart00633 Glyco_10 1.82e-101 19 307 1 263
Glycosyl hydrolase family 10.
cd00005 CBM9_like_1 6.60e-98 327 508 2 184
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 4.11e-76 3 309 51 339
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism].
pfam06452 CBM9_1 1.35e-74 336 508 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
ANY73387.1 0.0 1 953 390 1341
ANA80457.1 0.0 1 953 389 1328
AVV55472.1 0.0 1 953 389 1328
AWP30060.1 0.0 1 953 389 1328
AIQ22656.1 0.0 1 953 550 1485

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3RDK_A 2.94e-178 2 310 30 338
Proteincrystal structure of xylanase A1 of Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RDK_B Protein crystal structure of xylanase A1 of Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_A Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_B Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_C Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_D Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_E Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_F Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_G Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],3RO8_H Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],4E4P_A Second native structure of Xylanase A1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2],4E4P_B Second native structure of Xylanase A1 from Paenibacillus sp. JDR-2 [Paenibacillus sp. JDR-2]
3W24_A 2.27e-75 4 318 36 334
Thehigh-resolution crystal structure of TsXylA, intracellular xylanase from Thermoanaerobacterium saccharolyticum JW/SL-YS485 [Thermoanaerobacterium saccharolyticum JW/SL-YS485]
3W25_A 1.61e-74 4 318 36 334
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 1.61e-74 4 318 36 334
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 8.97e-61 4 308 40 339
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
C6CRV0 0.0 2 953 543 1461
Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
P38535 3.77e-114 4 948 237 1078
Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
P36917 2.32e-110 4 513 385 1047
Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1
Q60042 1.11e-93 3 508 391 1053
Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1
Q60037 1.97e-87 3 508 395 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

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
1.000062 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003402_03405.