CAZyme Information: MGYG000000346_02019

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae
• CAZyme ID: MGYG000000346_02019
• CAZy Family: GH43
• CAZyme Description: Xylan 1,3-beta-xylosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
439		49755.18	5.176

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000346	2294646	MAG	Sweden	Europe

• Gene Location: Start: 121; End: 1440 Strand: +

Full Sequence      

MSNPEWAKNLNTLEGGRGYWAPDISYYEGRFYITATFRLNDDGTVYRRQMVTSADRPEGP
YCEPVYLDEDGIDPSIFTDDDGRRYMLLNRGARIFEISPDGRKQLSEAELLYYGHQKRAP
EGSHLLKKDGWYYLFQAEGGTGIGHRISVARSRTLKGVYEPCPYNPIMRQLDEKGALQRC
GHGKPVCTPKGEWYMVYLCGRQLESSYTVLGRETAMDPITWTADGWPLVNNGQGPSVLQK
KPDLPEWIPAEGRENYVTPRVPDKGTIQLTENEIILRADTASLSTTEARSILVKRQKEFR
SIVETTVKIPADMMAGEEFGITCYYDENTYLTFGPSKTDEGIQLTLKEHVGDTDKVEGCI
SEKILPGTDLCLRVVTEGLRRSFYVKTEGADWECAAVLPRVDYLCDEGWHIGKRFTGAME
GIYARTCSAEERLIHFSRF

Enzyme Prediction     

No EC number prediction in MGYG000000346_02019.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	9	227	4.4e-60	0.7900355871886121

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08989	GH43_XYL-like	1.27e-113	2	222	52	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.
cd18617	GH43_XynB-like	2.94e-76	9	227	58	284	Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases 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. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. 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.
cd09000	GH43_SXA-like	2.17e-69	18	227	67	290	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	1.04e-64	4	227	53	281	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.
COG3507	XynB2	3.53e-62	16	424	88	529	Beta-xylosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABX41261.1	8.84e-203	1	424	183	614
CBL09363.1	1.60e-176	1	424	184	609
VCV21971.1	9.14e-176	1	424	184	609
CBL11992.1	1.29e-175	1	424	184	609
AUO18981.1	3.48e-156	1	424	185	617

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MS2_A	5.27e-100	9	424	89	517	Crystalstructure of the GH43 BlXynB protein from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]
6MS3_A	2.94e-99	9	424	89	517	Crystalstructure of the GH43 protein BlXynB mutant (K247S) from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580],6MS3_B Crystal structure of the GH43 protein BlXynB mutant (K247S) from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]
1YRZ_A	7.17e-54	18	439	73	521	ChainA, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125],1YRZ_B Chain B, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125]
1YI7_A	2.39e-46	18	439	72	530	Beta-d-xylosidase(selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824],1YI7_B Beta-d-xylosidase (selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824],1YI7_C Beta-d-xylosidase (selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824],1YI7_D Beta-d-xylosidase (selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824]
2EXI_A	4.11e-46	18	439	72	530	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A9ZND1	4.56e-49	9	439	64	530	Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1
P77713	3.16e-45	18	439	71	531	Putative beta-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yagH PE=3 SV=1
A7LXT8	1.38e-44	9	432	82	508	Non-reducing end alpha-L-arabinofuranosidase BoGH43A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02654 PE=1 SV=1
P94489	4.48e-39	18	439	71	528	Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynB PE=1 SV=2
P45982	4.70e-38	17	247	70	311	Xylosidase/arabinosidase OS=Butyrivibrio fibrisolvens OX=831 GN=xylB PE=3 SV=1

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
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000346_02019.