CAZyme Information: MGYG000004035_01796

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS1815
• CAZyme ID: MGYG000004035_01796
• CAZy Family: GH39
• CAZyme Description: Beta-xylosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
518		59751.88	5.73

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004035	2175802	MAG	United Kingdom	Europe

• Gene Location: Start: 1985; End: 3541 Strand: -

Full Sequence      

MITFRYTDKKFTDSIFHTVAIGRAYELLRHDLVQQLAEMQKELHFRYCRCHGLFHEDMAV
AIRKPDGTLGFQWHHMDKFIDNLLSVGLRPFFELGPMPYCMASDPKATIFHYEMNMSKPK
DYSEWYALCRAFTSHCVDRYGLDEVRTWFFEVWNEPNLDGFWPHGMEEYYILYTHAARAV
KSVDDALQVGGPASAGGMFIPEMIDYCCKNDVPLDFVSTHVYPIGEYCQFPERKNSPHAL
GGYMPTVVREVYERVQHSPMPHLPIYWTEWNTQYGKPGEAVTWTHNPSVDMHFAASSVLK
NVLETRDISDSMSYWTASDLFEEAGCPHSPFSCTYGLLTIHGVKKASYNAYKLLRKLRGR
EMAADTMEGAPFGCDVCATEENNVSRVLLYNWNALEIHDQPDWADSVKIPVREDGEYLIT
TAAIRKHKGSPYETWISMGSPHNLSPTQLELLRAHEEMDYDFISCTSQDGYVTVPFALKP
NEVLYMECEKKGDRIIPRAASKEDLDRWNKIMTLEELK

Enzyme Prediction     

EC	3.2.1.37

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH39	9	444	6.6e-116	0.9907192575406032

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01229	Glyco_hydro_39	1.59e-102	7	490	10	490	Glycosyl hydrolases family 39.
COG3664	XynB	6.08e-49	27	487	1	423	Beta-xylosidase [Carbohydrate transport and metabolism].
cd21510	agarase_cat	3.89e-04	119	222	76	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCG53665.1	3.00e-156	19	512	35	528
QTE39841.1	1.54e-95	2	490	35	526
ADQ03734.1	1.69e-95	16	484	17	475
QBE65339.1	1.17e-94	19	494	46	523
QGZ38676.1	1.39e-94	19	492	43	518

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4M29_A	1.55e-88	16	489	25	497	Structureof a GH39 Beta-xylosidase from Caulobacter crescentus [Caulobacter vibrioides CB15]
4EKJ_A	3.07e-88	16	489	25	497	ChainA, Beta-xylosidase [Caulobacter vibrioides]
6UQJ_A	4.10e-83	16	489	30	504	Crystalstructure of the GH39 enzyme from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306]
1PX8_A	8.90e-79	6	493	9	484	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	4.01e-77	9	493	12	485	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23552	4.21e-92	2	484	9	481	Beta-xylosidase OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=xynB PE=3 SV=1
O30360	6.84e-78	6	493	9	484	Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485) OX=1094508 GN=xynB PE=3 SV=1
P36906	1.03e-76	6	493	9	484	Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynB PE=1 SV=1
Q9ZFM2	1.06e-72	9	493	12	486	Beta-xylosidase OS=Geobacillus stearothermophilus OX=1422 GN=xynB PE=1 SV=1
P48441	2.58e-10	49	220	79	252	Alpha-L-iduronidase OS=Mus musculus OX=10090 GN=Idua PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004035_01796.