CAZyme Information: MGYG000000229_02018

Basic Information

• Species: CAG-317 sp000433215
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-317; CAG-317 sp000433215
• CAZyme ID: MGYG000000229_02018
• CAZy Family: GH43
• CAZyme Description: Beta-xylosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
348		40627.63	4.7682

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000229	2785689	Isolate	China	Asia

• Gene Location: Start: 121722; End: 122768 Strand: -

Full Sequence      

MTNHFFYSIFIYFFLVFYIIYEGDPKNPIVTSVPGESNERHDPDHLKPKYFNPDSVLQKS
GHGSYVETSLGEVYLVHLCSRPFAPELRCTLGRETTIQKMEWTEDGWLRMADGDNLAKEY
VEESKLPEYPVLQISDFDDFDSGELGNWYYVPHIMPQSFADVKARPWYVRIRGQESRTSL
NKVSILARKLTSVYAAVTTKMEYKPEVYQHSAGLIIYYDNMNYINLRKYYSQTLGGSALS
IIQLENGEKTEYLDTRIAVEDVPIYLRLQIEGRQLWFEWSYDGENYTRIGRTFDTTKFSD
EYCKYGEFTGTFVGLTCADRVLHKHYADFDFFSYEADEEKGMPAPEEK

Enzyme Prediction     

No EC number prediction in MGYG000000229_02018.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam17851	GH43_C2	1.02e-55	138	335	2	203	Beta xylosidase C-terminal Concanavalin A-like domain. This domain is found to the C-terminus of the pfam04616 domain. This domain adopts a concanavalin A-like fold.
COG3507	XynB2	1.82e-54	21	336	246	548	Beta-xylosidase [Carbohydrate transport and metabolism].
cd09000	GH43_SXA-like	1.60e-32	21	110	220	292	Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA. This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
pfam04616	Glyco_hydro_43	2.33e-14	21	107	214	280	Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd08989	GH43_XYL-like	4.78e-12	21	103	209	272	Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRT49145.1	3.24e-206	21	343	226	548
AWY98289.1	8.61e-194	21	342	225	546
APF21068.1	2.71e-187	21	342	132	453
QCU02864.1	2.44e-186	21	338	226	543
ANF15928.1	1.99e-185	21	342	226	547

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1YRZ_A	8.62e-67	21	334	226	523	ChainA, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125],1YRZ_B Chain B, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125]
2EXJ_A	1.13e-43	21	334	225	532	ChainA, beta-D-xylosidase [Geobacillus stearothermophilus],2EXJ_B Chain B, beta-D-xylosidase [Geobacillus stearothermophilus],2EXJ_C Chain C, beta-D-xylosidase [Geobacillus stearothermophilus],2EXJ_D Chain D, beta-D-xylosidase [Geobacillus stearothermophilus]
2EXI_A	1.13e-43	21	334	225	532	ChainA, beta-D-xylosidase [Geobacillus stearothermophilus],2EXI_B Chain B, beta-D-xylosidase [Geobacillus stearothermophilus],2EXI_C Chain C, beta-D-xylosidase [Geobacillus stearothermophilus],2EXI_D Chain D, beta-D-xylosidase [Geobacillus stearothermophilus]
2EXH_A	1.13e-43	21	334	225	532	Structureof the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus],2EXH_B Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus],2EXH_C Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus],2EXH_D Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus]
2EXK_A	1.13e-43	21	334	225	532	ChainA, beta-D-xylosidase [Geobacillus stearothermophilus],2EXK_B Chain B, beta-D-xylosidase [Geobacillus stearothermophilus],2EXK_C Chain C, beta-D-xylosidase [Geobacillus stearothermophilus],2EXK_D Chain D, beta-D-xylosidase [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P07129	2.72e-37	21	335	224	531	Beta-xylosidase OS=Bacillus pumilus OX=1408 GN=xynB PE=1 SV=2
P94489	1.83e-36	21	334	224	530	Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynB PE=1 SV=2
P77713	2.61e-36	53	335	239	534	Putative beta-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yagH PE=3 SV=1
A9ZND1	4.32e-34	21	334	227	532	Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.455379	0.538865	0.004012	0.000527	0.000402	0.000810

TMHMM  Annotations     

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5	22