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CAZyme Information: MGYG000003648_02615

You are here: Home > Sequence: MGYG000003648_02615

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 NK4A136 sp002314855
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; NK4A136; NK4A136 sp002314855
CAZyme ID MGYG000003648_02615
CAZy Family GH43
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
974 MGYG000003648_402|CGC1 109174.19 4.6117
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003648 3786163 MAG Fiji Oceania
Gene Location Start: 16481;  End: 19405  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.37 3.2.1.55

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH43 515 816 2.9e-121 0.9931972789115646

CDD Domains      download full data without filtering help

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.

CAZyme Hits      help

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

PDB Hits      download full data without filtering help

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]

Swiss-Prot Hits      download full data without filtering help

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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

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

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003648_02615.