CAZyme Information: MGYG000003172_00337

Basic Information

• Species: CAG-485 sp900555915
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900555915
• CAZyme ID: MGYG000003172_00337
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
705	MGYG000003172_35|CGC1	79357.77	5.2018

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003172	1933519	MAG	United States	North America

• Gene Location: Start: 4; End: 2121 Strand: +

Full Sequence      

MAVADSPVGPFRPQFRPIEGVAGIDPCVLVDDDGKSYIYWSGMGLSVAPLSDDMLHLAGS
PVRIEGLPEGFKEGPFAFKRDGRYYLTFPWVKDKTETLAYAMSDSPTGPFEFKGIIMDES
PTGCWTNHHSLVEKDGQWYLFYHHNDYSPDMDKRRSVRIDTVGFNSDGTIRKVTPTLRGV
GVCDARRRIEIDRYSDISPKGAGLRFVDEADKFKGWSVDLTRSGAWVRFDRVDFSSRPVR
EVRAMVKSQGGCRLKISDANGKEIATIKVPASEGWNVADAPVAYSPEGVADIKVSLVKGK
AEVDWIGFDMVPWESGAMSTGRYRNLFKELGYSDKDVADKLDEIFHGVFEGPDKVYFEAD
DNTAYISDIKNNDVRTEGMSYGMMIAVQLDKKEIFDRLWRWASKHMQHHGGPRDGYFAWS
CKTDGTRNSDGSASDGELYFITSLIFASNRWGNDTGIDYLAEARNILDKSMQKSGMEQVA
PLINLEHRLITFTPDPYGGTFTDPSYHIPVFYDIWAKWAGDGRSSFWKSCAEESRAFLHK
ATHPSTGLNPDYSTFDGKQRGANGFHSMFEAFRFDSWRVPMNIAIDYAWSGADAEWQRGY
ADRVQNFFYSQGIDTFVDQYNPDGTPVDKVLHAGESDSLRHSVGLVGTLGAVSLAATDVK
AKEFAQRLWDSRHEPYEDGYFDAYYDGLLRLFSFMLLSGNYRIIE

Enzyme Prediction     

No EC number prediction in MGYG000003172_00337.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH8	366	695	1.6e-82	0.93125
GH43	2	169	5.9e-62	0.6263736263736264

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08990	GH43_AXH_like	1.47e-66	1	172	92	269	Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, beta-xylosidase, endo-1,4-beta-xylanase, and alpha-L-arabinofuranosidase. This subgroup includes Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160), Butyrivibrio proteoclasticus alpha-L-arabinofuranosidase (Xsa43E;bpr_I2319), Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and metagenomic beta-xylosidase (EC 3.2.1.37) / alpha-L-arabinofuranosidase (EC 3.2.1.55) CoXyl43. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_AXH-like subgroup includes enzymes that have been characterized with beta-xylosidase, alpha-L-arabinofuranosidase, endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. 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. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43 shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. 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.
cd18618	GH43_Xsa43E-like	1.31e-49	2	172	96	275	Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase Xsa43E. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. 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. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. This subgroup includes Cellvibrio japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A, which confers its specificity by a surface cleft that is complementary to the helical backbone of the polysaccharide, and Butyrivibrio proteoclasticus GH43 enzyme Xsa43E, also an arabinofuranosidase, which has been shown to cleave arabinose side chains from short segments of xylan. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. 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.
COG3405	BcsZ	2.49e-49	323	703	8	350	Endo-1,4-beta-D-glucanase Y [Carbohydrate transport and metabolism].
cd18619	GH43_CoXyl43_like	1.69e-44	2	171	107	312	Glycosyl hydrolase family 43 protein such as metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. 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. Included in this subfamily is the metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43, which shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. 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.
cd18620	GH43_XylA-like	6.80e-43	1	171	93	273	Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium alpha-L-arabinofuranosidase XylA. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. 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. The GH43_XylA-like subgroup includes Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), endo-alpha-L-arabinanase (EC 3.2.1.-) as well as arabinoxylan arabinofuranohydrolase (AXH) activities. 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. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUU00913.1	0.0	1	704	132	835
QCD34665.1	0.0	1	704	133	837
AVM52698.1	0.0	1	704	132	836
AVM57873.1	0.0	1	704	132	836
QNT67600.1	0.0	1	705	128	836

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6SUD_A	7.10e-91	316	705	7	381	Structureof L320A mutant of Rex8A from Paenibacillus barcinonensis complexed with xylose. [Paenibacillus barcinonensis],6SUD_B Structure of L320A mutant of Rex8A from Paenibacillus barcinonensis complexed with xylose. [Paenibacillus barcinonensis]
6SRD_A	9.97e-91	316	705	7	381	Structureof Rex8A from Paenibacillus barcinonensis complexed with xylose. [Paenibacillus barcinonensis],6SRD_B Structure of Rex8A from Paenibacillus barcinonensis complexed with xylose. [Paenibacillus barcinonensis]
6TPP_A	7.64e-90	316	705	7	381	Structureof E70A mutant of Rex8A from Paenibacillus barcinonensis. [Paenibacillus barcinonensis],6TPP_B Structure of E70A mutant of Rex8A from Paenibacillus barcinonensis. [Paenibacillus barcinonensis]
6TO0_A	8.38e-90	316	705	7	381	Structureof E70A mutant of Rex8A from Paenibacillus barcinonensis complexed with 2(3)-alpha-L-arabinofuranosyl-xylotriose. [Paenibacillus barcinonensis],6TO0_B Structure of E70A mutant of Rex8A from Paenibacillus barcinonensis complexed with 2(3)-alpha-L-arabinofuranosyl-xylotriose. [Paenibacillus barcinonensis],6TOW_A Structure of E70A mutant of Rex8A from Paenibacillus barcinonensis complexed with xylotetraose. [Paenibacillus barcinonensis],6TOW_B Structure of E70A mutant of Rex8A from Paenibacillus barcinonensis complexed with xylotetraose. [Paenibacillus barcinonensis],6TRH_A Structure of E70A mutant of Rex8A from Paenibacillus barcinonensis complexed with 3(3)-alpha-L-arabinofuranosyl-xylotetraose. [Paenibacillus barcinonensis],6TRH_B Structure of E70A mutant of Rex8A from Paenibacillus barcinonensis complexed with 3(3)-alpha-L-arabinofuranosyl-xylotetraose. [Paenibacillus barcinonensis],6TRH_C Structure of E70A mutant of Rex8A from Paenibacillus barcinonensis complexed with 3(3)-alpha-L-arabinofuranosyl-xylotetraose. [Paenibacillus barcinonensis],6TRH_D Structure of E70A mutant of Rex8A from Paenibacillus barcinonensis complexed with 3(3)-alpha-L-arabinofuranosyl-xylotetraose. [Paenibacillus barcinonensis]
6SHY_A	1.51e-89	316	705	7	381	Structureof L320A/H321S double mutant of Rex8A from Paenibacillus barcinonensis [Paenibacillus barcinonensis],6SHY_B Structure of L320A/H321S double mutant of Rex8A from Paenibacillus barcinonensis [Paenibacillus barcinonensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A0S2UQQ5	1.01e-89	316	703	7	379	Reducing-end xylose-releasing exo-oligoxylanase Rex8A OS=Paenibacillus barcinonensis OX=198119 GN=rex8A PE=1 SV=1
Q9KB30	1.60e-86	316	703	7	378	Reducing end xylose-releasing exo-oligoxylanase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=BH2105 PE=1 SV=1
A1A048	3.23e-75	325	702	14	377	Reducing end xylose-releasing exo-oligoxylanase OS=Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) OX=367928 GN=xylA PE=1 SV=1
P37701	9.28e-30	371	701	93	389	Endoglucanase 2 OS=Ruminiclostridium josui OX=1499 GN=celB PE=3 SV=1
A3DC29	1.65e-28	371	701	89	388	Endoglucanase A OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celA PE=1 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
1.000040	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003172_00337.