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CAZyme Information: MGYG000004172_01474

You are here: Home > Sequence: MGYG000004172_01474

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; ;
CAZyme ID MGYG000004172_01474
CAZy Family GH39
CAZyme Description Beta-xylosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
545 MGYG000004172_5|CGC4 62206.48 5.5524
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004172 3050906 MAG United Kingdom Europe
Gene Location Start: 192042;  End: 193679  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004172_01474.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH39 68 497 7.6e-67 0.925754060324826

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01229 Glyco_hydro_39 4.47e-33 69 543 39 488
Glycosyl hydrolases family 39.
COG3664 XynB 1.36e-16 113 544 34 426
Beta-xylosidase [Carbohydrate transport and metabolism].
cd21510 agarase_cat 0.002 163 275 62 187
alpha-beta barrel catalytic domain of agarase, such as GH86-like endo-acting agarases identified in non-marine organisms. Typically, agarases (E.C. 3.2.1.81) are found in ocean-dwelling bacteria since agarose is a principle component of red algae cell wall polysaccharides. Agarose is a linear polymer of alternating D-galactose and 3,6-anhydro-L-galactopyranose. Endo-acting agarases, such as glycoside hydrolase 16 (GH16) and GH86 hydrolyze internal beta-1,4 linkages. GH86-like endo-acting agarase of this protein family has been identified in the human intestinal bacterium Bacteroides uniformis. This acquired metabolic pathway, as demonstrated by the prevalence of agar-specific genetic cluster called polysaccharide utilization loci (PULs), varies considerably between human populations, being much more prevalent in a Japanese sample than in North America, European, or Chinese samples. Agarase activity was also identified in the non-marine bacterium Cellvibrio sp.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QGY46243.1 1.38e-144 33 543 25 537
QBI00783.1 2.52e-69 16 543 16 564
QCP10850.1 2.62e-68 16 543 16 564
QBE65838.1 1.52e-64 16 543 16 564
QYF91718.1 2.15e-57 6 543 3 560

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4M29_A 4.08e-42 35 496 13 449
Structureof a GH39 Beta-xylosidase from Caulobacter crescentus [Caulobacter vibrioides CB15]
4EKJ_A 7.72e-42 35 496 13 449
ChainA, Beta-xylosidase [Caulobacter vibrioides]
6UQJ_A 3.89e-29 50 544 34 505
Crystalstructure of the GH39 enzyme from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306]
2BS9_A 3.04e-28 62 542 32 480
Nativecrystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_B Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_C Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_D Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_E Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_F Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_G Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus],2BS9_H Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
1W91_A 4.10e-28 62 542 32 480
crystalstructure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_B crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_C crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_D crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_E crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_F crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_G crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct],1W91_H crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from Seleniomethionine [synthetic construct]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9ZFM2 8.10e-26 62 542 32 481
Beta-xylosidase OS=Geobacillus stearothermophilus OX=1422 GN=xynB PE=1 SV=1
P23552 9.56e-26 28 515 4 457
Beta-xylosidase OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=xynB PE=3 SV=1
O30360 4.92e-24 62 543 32 480
Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485) OX=1094508 GN=xynB PE=3 SV=1
P36906 6.91e-23 62 543 32 480
Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynB PE=1 SV=1
P48441 6.56e-14 171 542 141 530
Alpha-L-iduronidase OS=Mus musculus OX=10090 GN=Idua PE=1 SV=2

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
0.000248 0.999140 0.000156 0.000159 0.000146 0.000137

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004172_01474.