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CAZyme Information: MGYG000002196_00482

You are here: Home > Sequence: MGYG000002196_00482

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 UBA1691 sp900552985
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA1691; UBA1691 sp900552985
CAZyme ID MGYG000002196_00482
CAZy Family GH39
CAZyme Description Beta-xylosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
525 MGYG000002196_15|CGC1 59801.6 5.1017
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002196 2479856 MAG Spain Europe
Gene Location Start: 23995;  End: 25572  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.37

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH39 13 478 2.6e-124 0.9930394431554525

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01229 Glyco_hydro_39 9.04e-128 2 512 1 478
Glycosyl hydrolases family 39.
COG3664 XynB 6.64e-53 31 519 1 422
Beta-xylosidase [Carbohydrate transport and metabolism].
cd21510 agarase_cat 1.14e-07 115 255 65 205
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.
COG2723 BglB 0.006 82 208 103 236
Beta-glucosidase/6-phospho-beta-glucosidase/beta-galactosidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CDZ24727.1 2.10e-150 1 522 1 491
ADQ45468.1 6.28e-139 15 524 14 480
ADQ03734.1 7.37e-138 2 521 1 477
AZT91388.1 6.11e-137 2 525 1 482
BCS82259.1 8.36e-137 2 496 1 453

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4M29_A 8.23e-78 14 521 21 496
Structureof a GH39 Beta-xylosidase from Caulobacter crescentus [Caulobacter vibrioides CB15]
4EKJ_A 1.62e-77 14 521 21 496
ChainA, Beta-xylosidase [Caulobacter vibrioides]
1PX8_A 2.60e-75 1 521 1 479
Crystalstructure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase [Thermoanaerobacterium saccharolyticum],1PX8_B Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase [Thermoanaerobacterium saccharolyticum],1UHV_A Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase [Thermoanaerobacterium saccharolyticum],1UHV_B Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase [Thermoanaerobacterium saccharolyticum],1UHV_C Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase [Thermoanaerobacterium saccharolyticum],1UHV_D Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase [Thermoanaerobacterium saccharolyticum]
2BS9_A 5.88e-74 12 490 11 449
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 8.25e-74 12 490 11 449
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
P23552 2.88e-137 1 525 6 487
Beta-xylosidase OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=xynB PE=3 SV=1
P36906 2.80e-74 1 521 1 479
Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynB PE=1 SV=1
O30360 2.99e-73 1 521 1 479
Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485) OX=1094508 GN=xynB PE=3 SV=1
Q9ZFM2 6.49e-73 12 485 11 446
Beta-xylosidase OS=Geobacillus stearothermophilus OX=1422 GN=xynB PE=1 SV=1
T2KM23 2.49e-14 118 233 158 270
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
1.000046 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002196_00482.