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CAZyme Information: MGYG000002621_00487

You are here: Home > Sequence: MGYG000002621_00487

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Bacteroides ndongoniae
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides ndongoniae
CAZyme ID MGYG000002621_00487
CAZy Family GH43
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
837 MGYG000002621_3|CGC4 95584.08 6.332
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002621 3633256 MAG China Asia
Gene Location Start: 193513;  End: 196026  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002621_00487.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH43 30 299 6.9e-116 0.9963369963369964
GH8 500 825 2e-81 0.925

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08990 GH43_AXH_like 1.78e-123 31 302 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 1.42e-91 23 301 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 9.93e-87 29 302 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 4.53e-76 31 300 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 2.76e-71 31 303 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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVM57873.1 0.0 12 837 12 840
AVM52698.1 0.0 12 837 12 840
QUU00913.1 0.0 11 836 11 838
QCD34665.1 0.0 20 837 23 841
QNT67600.1 0.0 10 836 8 838

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6SUD_A 2.53e-94 446 832 6 379
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 3.55e-94 446 832 6 379
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 2.68e-93 446 832 6 379
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 2.94e-93 446 832 6 379
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 3.75e-93 446 832 6 379
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      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0A0S2UQQ5 1.83e-93 446 832 6 379
Reducing-end xylose-releasing exo-oligoxylanase Rex8A OS=Paenibacillus barcinonensis OX=198119 GN=rex8A PE=1 SV=1
Q9KB30 3.46e-92 446 836 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 1.29e-71 456 831 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 4.11e-59 24 300 8 317
Xylosidase/arabinosidase OS=Bacteroides ovatus OX=28116 GN=xsa PE=2 SV=1
P48791 2.51e-49 29 303 11 318
Beta-xylosidase OS=Prevotella ruminicola OX=839 GN=xynB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000215 0.999223 0.000146 0.000141 0.000128 0.000123

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002621_00487.