CAZyme Information: MGYG000000553_00605

Basic Information

• Species: Prevotella sp900548535
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900548535
• CAZyme ID: MGYG000000553_00605
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
842	MGYG000000553_3|CGC3	95754.55	6.7806

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000553	2921999	MAG	China	Asia

• Gene Location: Start: 137583; End: 140111 Strand: +

Full Sequence      

MNIKKTLFCALACTVEVAALAQNPIINSQFTADPTARVFNGKIYLYPSHDIPSPIEKLKT
WFCMPDYHVFSSSNLTDWEDHGVIVSQDKVPWVQDGSYTMWAPDCVCKDGKYYFYFPAAP
KGEEKGFGVGVAIADHPEGPFMPMWKPIEGIHGIDPCVLIDRDGQAYIYWAGMGLHMAKL
KPNMMELASEPQAVEGLPEGFKEGPFAFERNGKYYFTFPWVREKDGTETLAYAMADHPMG
PFTFKGVIMDESPTKCWTNHHSIVEYQGQWYLFYHHNDYSPQFDKNRSVRIDSLNFNPDG
TIQKVIPTLRGVGLTKARSHIQIDRYSALQGKGIGIDYLDKNNCFAGWKTLFSKSNTALI
YNKVDFGNEEVEEITVRAKSPKGGVLVVRADGKKGNIIAKVKIPKSAAWKNVRAQVLHAP
LGVHALHVSLQSGADVEVDWLGFDALPWEKGAFETHQYRNLFAEMGYRQADIDKKLNEVF
HDVFYGKNKVYFEVGDSMGYVSDVKNNDVRTEGMSYGMMAAVQFGKKDIFDRLWRWSKRY
MQHQKGPYKGYFAWSCKTDGTRNAQGAASDGELYFVTSLIFASNRWGNDTGINYLKEAQN
ILDCSMQKVGMDRTAPLINLEHQLITFTPDHWGGKFTDPSYHLPAFYEVWAKWANDGRSQ
FWKECAEKSREFLHKCINEKTGLNPDYCNYDGSLMKTGQLLGDAFRYDSWRVPMNIALDY
SWACKDKEWQQKYANTLQNFLYSQGIDSFLDQYNVDGTMVEDILPAGTAPEALRHSIGFV
ATAAAASLVSNHVKGREFVSHFWNAKHEPDKEGFFDGYYDGLLRLFAFMHLSGRYQIIEP
QK

Enzyme Prediction     

No EC number prediction in MGYG000000553_00605.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	31	301	4.5e-113	0.9963369963369964
GH8	501	830	2.3e-84	0.934375

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08990	GH43_AXH_like	1.37e-124	32	304	1	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.
cd18619	GH43_CoXyl43_like	1.09e-94	24	303	1	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.
cd18618	GH43_Xsa43E-like	2.53e-87	30	304	1	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.
cd18620	GH43_XylA-like	1.58e-81	32	302	1	272	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.
cd09004	GH43_bXyl-like	3.76e-70	32	305	1	266	Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675) and (BT3662;BT_3662); includes mostly xylanases. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. 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
QNT67600.1	0.0	5	841	2	838
AVM57873.1	0.0	10	842	11	840
AVM52698.1	0.0	10	842	11	840
QUU00913.1	0.0	13	841	14	838
QCD34665.1	0.0	19	840	21	839

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6SUD_A	1.14e-92	450	839	6	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	2.23e-92	450	839	6	381	Structureof Rex8A from Paenibacillus barcinonensis complexed with xylose. [Paenibacillus barcinonensis],6SRD_B Structure of Rex8A from Paenibacillus barcinonensis complexed with xylose. [Paenibacillus barcinonensis]
6SHY_A	1.19e-91	450	839	6	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]
6TPP_A	1.67e-91	450	839	6	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	1.83e-91	450	839	6	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A0S2UQQ5	2.24e-91	450	837	6	379	Reducing-end xylose-releasing exo-oligoxylanase Rex8A OS=Paenibacillus barcinonensis OX=198119 GN=rex8A PE=1 SV=1
Q9KB30	6.74e-87	450	841	6	382	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	1.92e-73	460	836	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
P49943	1.64e-59	25	302	8	317	Xylosidase/arabinosidase OS=Bacteroides ovatus OX=28116 GN=xsa PE=2 SV=1
P48791	1.28e-52	25	305	6	318	Beta-xylosidase OS=Prevotella ruminicola OX=839 GN=xynB PE=3 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
0.000651	0.998393	0.000367	0.000195	0.000177	0.000168

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000553_00605.