CAZyme Information: MGYG000002832_00057

Basic Information

• Species: Prevotella sp900548195
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900548195
• CAZyme ID: MGYG000002832_00057
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1049	MGYG000002832_2|CGC1	119738.49	7.1766

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002832	2701309	MAG	United Republic of Tanzania	Africa

• Gene Location: Start: 8398; End: 11547 Strand: -

Full Sequence      

MTILKQIAIMSILATAVSATKAQNPIINHQFSADPTARVFNGRIYLFPSHDIISPVEPEK
KWFSMADYHVFSSDNLTDWTDHGVILSQEQVPWGNPKAYSMWAPDCVEKDGKYYFFFPDA
PKPLATDKDARSRGFGIGVATADHPYGPYKALPDNIKGIAGIDPCVLQASNGENVIFWGG
GGLRMARLKDNLIELADEEMQNPTEAPNGMKFYGHAVEGLPEGFKEGPFAFERNGKFYLT
YPWVRKENGTECLAYAMSDKPMGPYEYKGIIMKEHENGCWTNHHSIVEYKGQWYLFYHNN
AYSPWFDKNRSVCADSLFFNPDGTIQEVKPTLRGIGVTDARTMVQMDRYSSIGGGATIEY
NDTTNRFLGWKTILPKDGFVTYANVQIPEGEYTVWVNKPGFWGRAEIVDIRKTTLELKVN
KLPNGLHELVLTNKGKAPVEVDWISLNPRTPLVPSSSGGLATGTYRNLFVEAGHSEAEVE
AKLRQVFDDVFKGKNRCYFEAGKDMAYISDLKNKDVRTEGMSYGMMIAVQFDRKDIFDRL
WRWSKKYMQMQDGPMKGYFRWSCKPDGTPNANGPASDGELYYITSLIFASNRWGNSGEID
YLKEAQYILDCIQPRQTEFTMRRGMDGKRLEKPVTTKRTVSLIDPETDLITFVPGVSFTD
PSYHIPAFYEVWARYAEDGRASYWRECARKSREYLHKSVHPLTGLNDDYNNFDGTPLHNN
RLLGDCFRYDSWRVPMNIALDYSWACSDRQWQQNYGHTIQNFFFSQGIDSYLDQYNTDGT
LPKQILPAGTYQPKLRHSIGLMATLAASSIMCSHPKSYDFIDRLWNAKHKPDADGYFDAY
YDGLLRLFAFMHLSGHYRVIEKTPQLETYLRPATKDSTTPDSEGFVRRWMLHDPISKPNR
SNTVFTDTYLNETFPQPLAYSKKDKAWNAYDSQLFNVKLYRLATCTGQQRYGVIFWATTI
IECDEEIKDVRFAIGSNSASKWWLNGQEMAMLSGDRRMVRDDVVSRPVTLKKGRNIITGA
VINGPGMSDFCFRIVDADKYNLRISTAFR

Enzyme Prediction     

No EC number prediction in MGYG000002832_00057.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	32	324	5.6e-102	0.9963369963369964
GH8	511	852	1.9e-73	0.925

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08990	GH43_AXH_like	7.91e-111	33	326	1	268	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	1.70e-84	25	326	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	6.55e-81	31	327	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	2.89e-74	33	327	1	274	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	1.93e-63	33	328	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
QNO39517.1	0.0	13	1043	11	1041
AVM52698.1	0.0	19	860	19	836
AVM57873.1	0.0	19	860	19	836
QNT67600.1	0.0	8	861	7	836
QUU00913.1	0.0	21	860	21	835

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5YXT_A	7.18e-90	458	859	6	375	Glycosidehydrolase family 8 Xylanase [Paenibacillus barengoltzii G22],5YXT_B Glycoside hydrolase family 8 Xylanase [Paenibacillus barengoltzii G22],5YXT_C Glycoside hydrolase family 8 Xylanase [Paenibacillus barengoltzii G22],5YXT_D Glycoside hydrolase family 8 Xylanase [Paenibacillus barengoltzii G22]
6SUD_A	1.37e-87	455	862	4	382	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	1.90e-87	455	862	4	382	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	1.36e-86	455	862	4	382	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	1.49e-86	455	862	4	382	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	1.88e-86	455	859	4	379	Reducing-end xylose-releasing exo-oligoxylanase Rex8A OS=Paenibacillus barcinonensis OX=198119 GN=rex8A PE=1 SV=1
Q9KB30	3.05e-81	455	859	4	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	7.04e-70	467	858	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	1.23e-46	31	325	13	317	Xylosidase/arabinosidase OS=Bacteroides ovatus OX=28116 GN=xsa PE=2 SV=1
P48791	2.26e-45	31	329	11	319	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
0.001419	0.997125	0.000750	0.000252	0.000214	0.000203

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002832_00057.