logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002719_02068

You are here: Home > Sequence: MGYG000002719_02068

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; HGM11514; HGM11514; ;
CAZyme ID MGYG000002719_02068
CAZy Family GH39
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
478 54488.99 4.9992
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002719 3080250 MAG Canada North America
Gene Location Start: 2402;  End: 3838  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002719_02068.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH39 13 391 4.4e-145 0.888631090487239

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01229 Glyco_hydro_39 2.66e-123 4 382 3 385
Glycosyl hydrolases family 39.
COG3664 XynB 1.17e-73 31 478 1 427
Beta-xylosidase [Carbohydrate transport and metabolism].
cd21510 agarase_cat 3.83e-04 152 225 101 187
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
QEE50839.1 8.03e-157 1 477 39 535
ADL51184.1 2.23e-156 1 478 327 820
BAV13115.1 3.03e-156 1 478 338 831
QNR85653.1 2.14e-155 2 477 34 529
AEV98716.1 3.19e-155 2 477 24 520

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4M29_A 2.08e-133 2 475 9 496
Structureof a GH39 Beta-xylosidase from Caulobacter crescentus [Caulobacter vibrioides CB15]
4EKJ_A 2.94e-133 2 475 9 496
ChainA, Beta-xylosidase [Caulobacter vibrioides]
6UQJ_A 3.73e-119 2 475 14 503
Crystalstructure of the GH39 enzyme from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306]
1W91_A 1.85e-96 22 379 21 384
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 1.85e-96 22 379 21 384
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P23552 5.64e-107 13 377 18 386
Beta-xylosidase OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=xynB PE=3 SV=1
Q9ZFM2 3.36e-97 22 379 21 386
Beta-xylosidase OS=Geobacillus stearothermophilus OX=1422 GN=xynB PE=1 SV=1
P36906 5.47e-91 15 379 14 383
Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynB PE=1 SV=1
O30360 3.04e-90 15 379 14 383
Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485) OX=1094508 GN=xynB PE=3 SV=1
Q01634 6.65e-15 48 228 83 266
Alpha-L-iduronidase OS=Canis lupus familiaris OX=9615 GN=IDUA 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
1.000054 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002719_02068.