Species | NK4A136 sp002314855 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; NK4A136; NK4A136 sp002314855 | |||||||||||
CAZyme ID | MGYG000003648_02615 | |||||||||||
CAZy Family | GH43 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 16481; End: 19405 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH43 | 515 | 816 | 2.9e-121 | 0.9931972789115646 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd18620 | GH43_XylA-like | 5.61e-140 | 525 | 825 | 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. |
COG2272 | PnbA | 5.35e-96 | 4 | 483 | 4 | 468 | Carboxylesterase type B [Lipid transport and metabolism]. |
pfam00135 | COesterase | 4.89e-95 | 4 | 477 | 4 | 490 | Carboxylesterase family. |
cd00312 | Esterase_lipase | 1.70e-91 | 4 | 472 | 1 | 474 | Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate. |
cd08990 | GH43_AXH_like | 2.44e-57 | 526 | 825 | 2 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AOZ95200.1 | 0.0 | 1 | 974 | 1 | 925 |
ADL33049.1 | 0.0 | 1 | 974 | 1 | 970 |
VCV24166.1 | 9.37e-255 | 510 | 971 | 2 | 463 |
ADZ83008.1 | 5.48e-246 | 510 | 967 | 2 | 459 |
VCV24062.1 | 1.04e-241 | 510 | 967 | 2 | 459 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6EMI_A | 2.83e-57 | 4 | 471 | 8 | 498 | Crystalstructure of a variant of human butyrylcholinesterase expressed in bacteria. [Homo sapiens],6EMI_B Crystal structure of a variant of human butyrylcholinesterase expressed in bacteria. [Homo sapiens] |
5HQ3_A | 1.17e-53 | 4 | 472 | 10 | 504 | Stable,high-expression variant of human acetylcholinesterase [Homo sapiens] |
5HQ3_B | 1.20e-53 | 4 | 472 | 10 | 504 | Stable,high-expression variant of human acetylcholinesterase [Homo sapiens] |
5K5E_A | 3.75e-53 | 4 | 470 | 5 | 494 | Discoveryand Structure-Activity Relationships of a Highly Selective Butyrylcholinesterase Inhibitor by Structure-Based Virtual Screening [Homo sapiens],5K5E_B Discovery and Structure-Activity Relationships of a Highly Selective Butyrylcholinesterase Inhibitor by Structure-Based Virtual Screening [Homo sapiens],6ESJ_A Human butyrylcholinesterase in complex with propidium [Homo sapiens],6ESJ_B Human butyrylcholinesterase in complex with propidium [Homo sapiens],6ESY_A Human butyrylcholinesterase in complex with thioflavine T [Homo sapiens],6ESY_B Human butyrylcholinesterase in complex with thioflavine T [Homo sapiens],6F7Q_A Human Butyrylcholinesterase complexed with N-Propargyliperidines [Homo sapiens],6F7Q_B Human Butyrylcholinesterase complexed with N-Propargyliperidines [Homo sapiens] |
5DYW_A | 3.82e-53 | 4 | 470 | 6 | 495 | Crystalstructure of human butyrylcholinesterase in complex with N-((1-benzylpiperidin-3-yl)methyl)-N-(2-methoxyethyl)naphthalene-2-sulfonamide [Homo sapiens],5DYW_B Crystal structure of human butyrylcholinesterase in complex with N-((1-benzylpiperidin-3-yl)methyl)-N-(2-methoxyethyl)naphthalene-2-sulfonamide [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P48790 | 1.03e-222 | 510 | 968 | 2 | 466 | Xylosidase/arabinosidase OS=Thermoclostridium stercorarium OX=1510 GN=xylA PE=1 SV=1 |
O62760 | 9.63e-57 | 4 | 508 | 33 | 549 | Cholinesterase OS=Felis catus OX=9685 GN=BCHE PE=2 SV=1 |
O62761 | 2.42e-56 | 4 | 508 | 33 | 549 | Cholinesterase OS=Panthera tigris tigris OX=74535 GN=BCHE PE=2 SV=1 |
P81908 | 9.07e-54 | 4 | 470 | 5 | 494 | Cholinesterase OS=Equus caballus OX=9796 GN=BCHE PE=1 SV=1 |
P32749 | 2.76e-53 | 4 | 470 | 33 | 522 | Cholinesterase OS=Bos taurus OX=9913 GN=BCHE PE=2 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000058 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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