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CAZyme Information: MGYG000000574_00123

You are here: Home > Sequence: MGYG000000574_00123

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; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; ;
CAZyme ID MGYG000000574_00123
CAZy Family GH39
CAZyme Description Beta-xylosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
513 59160.69 5.8766
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000574 5306470 MAG Madagascar Africa
Gene Location Start: 5004;  End: 6545  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.37

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH39 17 469 1.8e-112 0.9814385150812065

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01229 Glyco_hydro_39 3.65e-97 1 512 1 487
Glycosyl hydrolases family 39.
COG3664 XynB 1.71e-43 31 513 2 425
Beta-xylosidase [Carbohydrate transport and metabolism].
COG2723 BglB 0.001 92 203 104 220
Beta-glucosidase/6-phospho-beta-glucosidase/beta-galactosidase [Carbohydrate transport and metabolism].
cd21510 agarase_cat 0.004 131 208 72 152
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
QYN52656.1 4.91e-117 9 494 7 467
QYN58463.1 1.96e-116 9 494 7 467
AST58227.1 2.48e-114 2 513 3 476
ADL68219.1 2.48e-114 2 513 3 476
QYN56463.1 3.91e-113 5 500 6 473

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6UQJ_A 1.03e-77 3 513 16 504
Crystalstructure of the GH39 enzyme from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306]
1W91_A 7.39e-76 17 513 17 481
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]
2BS9_A 1.04e-75 17 513 17 481
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]
4M29_A 3.72e-75 3 513 11 497
Structureof a GH39 Beta-xylosidase from Caulobacter crescentus [Caulobacter vibrioides CB15]
4EKJ_A 7.33e-75 3 513 11 497
ChainA, Beta-xylosidase [Caulobacter vibrioides]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P23552 4.13e-101 1 513 7 486
Beta-xylosidase OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=xynB PE=3 SV=1
Q9ZFM2 4.44e-74 17 513 17 482
Beta-xylosidase OS=Geobacillus stearothermophilus OX=1422 GN=xynB PE=1 SV=1
P36906 1.50e-68 10 509 3 476
Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynB PE=1 SV=1
O30360 8.90e-66 10 509 3 476
Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485) OX=1094508 GN=xynB PE=3 SV=1
T2KM23 5.16e-12 128 265 159 306
Alpha-1,4-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22200 PE=2 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
1.000067 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000574_00123.