Species | Bifidobacterium pullorum | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium pullorum | |||||||||||
CAZyme ID | MGYG000001159_01264 | |||||||||||
CAZy Family | GH10 | |||||||||||
CAZyme Description | Endo-1,4-beta-xylanase A | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 27464; End: 29341 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH10 | 2 | 196 | 1.9e-50 | 0.5775577557755776 |
CBM9 | 382 | 558 | 1.6e-41 | 0.9945054945054945 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00005 | CBM9_like_1 | 5.11e-54 | 400 | 558 | 28 | 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. |
smart00633 | Glyco_10 | 9.59e-50 | 2 | 193 | 83 | 260 | Glycosyl hydrolase family 10. |
pfam00331 | Glyco_hydro_10 | 1.24e-45 | 2 | 193 | 125 | 305 | Glycosyl hydrolase family 10. |
pfam06452 | CBM9_1 | 7.41e-37 | 404 | 558 | 26 | 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. |
COG3693 | XynA | 8.80e-32 | 2 | 193 | 148 | 334 | Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QGM62627.1 | 0.0 | 1 | 625 | 198 | 818 |
BAQ29203.1 | 0.0 | 1 | 625 | 198 | 818 |
QSY56935.1 | 1.47e-216 | 1 | 571 | 203 | 778 |
AGW85589.1 | 4.70e-191 | 1 | 570 | 178 | 753 |
AZC13060.1 | 3.45e-144 | 1 | 567 | 512 | 1050 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3W24_A | 2.86e-29 | 1 | 193 | 143 | 320 | Thehigh-resolution crystal structure of TsXylA, intracellular xylanase from Thermoanaerobacterium saccharolyticum JW/SL-YS485 [Thermoanaerobacterium saccharolyticum JW/SL-YS485] |
1I82_A | 7.46e-29 | 388 | 559 | 17 | 188 | Family9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a With Cellobiose [Thermotoga maritima],1I8A_A Family 9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a With Glucose [Thermotoga maritima],1I8U_A Family 9 Carbohydrate-Binding Module From Thermotoga Maritima Xylanase 10a [Thermotoga maritima] |
3W25_A | 1.79e-28 | 1 | 193 | 143 | 320 | 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 | 1.79e-28 | 1 | 193 | 143 | 320 | 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 | 3.49e-28 | 1 | 193 | 150 | 335 | Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P38535 | 2.12e-66 | 1 | 563 | 344 | 899 | Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1 |
P36917 | 5.45e-64 | 1 | 563 | 492 | 1047 | Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1 |
Q60042 | 1.64e-61 | 4 | 559 | 494 | 1054 | Endo-1,4-beta-xylanase A OS=Thermotoga neapolitana OX=2337 GN=xynA PE=1 SV=1 |
Q60037 | 1.61e-57 | 4 | 559 | 498 | 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 |
O69230 | 3.06e-48 | 1 | 559 | 499 | 1084 | Endo-1,4-beta-xylanase C OS=Paenibacillus barcinonensis OX=198119 GN=xynC PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.998952 | 0.001082 | 0.000015 | 0.000003 | 0.000001 | 0.000003 |
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