dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000000042_00937

You are here: Home > Sequence: MGYG000000042_00937

Basic Information help

Species

Phocaeicola sp900066445

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900066445

CAZyme ID

MGYG000000042_00937

CAZy Family

GH39

CAZyme Description

Beta-xylosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
513	MGYG000000042_2\|CGC8	59783.12	7.0008

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000042	3613218	Isolate	United Kingdom	Europe

Gene Location

Start: 340754; End: 342295 Strand: +

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.37

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH39	32	466	1e-148	0.9907192575406032

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01229	Glyco_hydro_39	3.31e-129	24	484	3	461	Glycosyl hydrolases family 39.
COG3664	XynB	1.78e-72	51	510	2	424	Beta-xylosidase [Carbohydrate transport and metabolism].
cd21510	agarase_cat	6.20e-08	131	243	57	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
AXP80098.1	2.06e-185	19	511	30	528
QBN17883.1	2.73e-185	22	511	32	526
SDT44124.1	7.73e-180	17	510	28	525
SDT04047.1	1.74e-179	22	510	57	549
QEE50839.1	1.16e-178	21	511	39	534

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6UQJ_A	4.63e-124	22	511	14	504	Crystalstructure of the GH39 enzyme from Xanthomonas axonopodis pv. citri [Xanthomonas citri pv. citri str. 306]
4M29_A	1.83e-121	22	511	9	497	Structureof a GH39 Beta-xylosidase from Caulobacter crescentus [Caulobacter vibrioides CB15]
4EKJ_A	3.65e-121	22	511	9	497	ChainA, Beta-xylosidase [Caulobacter vibrioides]
2BS9_A	5.44e-106	23	511	3	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]
1W91_A	4.29e-105	22	511	2	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9ZFM2	1.71e-104	22	406	2	394	Beta-xylosidase OS=Geobacillus stearothermophilus OX=1422 GN=xynB PE=1 SV=1
P23552	1.32e-102	19	498	2	473	Beta-xylosidase OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=xynB PE=3 SV=1
P36906	1.05e-101	21	511	4	480	Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynB PE=1 SV=1
O30360	4.15e-101	38	511	18	480	Beta-xylosidase OS=Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485) OX=1094508 GN=xynB PE=3 SV=1
P48441	2.88e-12	67	244	74	255	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
0.000209	0.999197	0.000144	0.000142	0.000129	0.000128

TMHMM Annotations help

There is no transmembrane helices in MGYG000000042_00937.