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CAZyme Information: MGYG000004860_01425

You are here: Home > Sequence: MGYG000004860_01425

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 Levilactobacillus namurensis
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Levilactobacillus; Levilactobacillus namurensis
CAZyme ID MGYG000004860_01425
CAZy Family GH43
CAZyme Description Beta-xylosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
541 MGYG000004860_11|CGC1 61574.04 4.6781
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004860 2610545 MAG China Asia
Gene Location Start: 30744;  End: 32369  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.37 3.2.1.55 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH43 3 304 3.7e-134 0.9965753424657534

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3507 XynB2 0.0 1 538 19 549
Beta-xylosidase [Carbohydrate transport and metabolism].
cd09000 GH43_SXA-like 0.0 5 306 1 292
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA. This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These 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. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. 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.
cd08989 GH43_XYL-like 2.35e-109 5 299 1 272
Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). 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.
cd18617 GH43_XynB-like 5.78e-109 5 304 1 284
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These 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. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. 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.
pfam04616 Glyco_hydro_43 4.39e-104 3 304 1 281
Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. 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
QFR62197.1 0.0 1 541 1 541
AKP64559.1 0.0 1 540 1 540
QCZ49544.1 0.0 1 540 1 540
AGT14431.1 0.0 1 540 1 540
SQG82162.1 0.0 1 540 1 540

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1Y7B_A 7.32e-200 3 539 4 536
Beta-d-xylosidase,A Family 43 Glycoside Hydrolase [Clostridium acetobutylicum ATCC 824],1Y7B_B Beta-d-xylosidase, A Family 43 Glycoside Hydrolase [Clostridium acetobutylicum ATCC 824],1Y7B_C Beta-d-xylosidase, A Family 43 Glycoside Hydrolase [Clostridium acetobutylicum ATCC 824],1Y7B_D Beta-d-xylosidase, A Family 43 Glycoside Hydrolase [Clostridium acetobutylicum ATCC 824]
1YI7_A 1.19e-198 3 539 4 536
Beta-d-xylosidase(selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824],1YI7_B Beta-d-xylosidase (selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824],1YI7_C Beta-d-xylosidase (selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824],1YI7_D Beta-d-xylosidase (selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824]
3C2U_A 3.91e-196 1 538 1 537
Structureof the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane [Selenomonas ruminantium],3C2U_B Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane [Selenomonas ruminantium],3C2U_C Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane [Selenomonas ruminantium],3C2U_D Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane [Selenomonas ruminantium]
2EXH_A 7.46e-183 2 538 3 535
Structureof the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus],2EXH_B Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus],2EXH_C Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus],2EXH_D Structure of the family43 beta-Xylosidase from geobacillus stearothermophilus [Geobacillus stearothermophilus]
1YIF_A 9.88e-183 1 537 1 532
CRYSTALSTRUCTURE OF beta-1,4-xylosidase FROM BACILLUS SUBTILIS, NEW YORK STRUCTURAL GENOMICS CONSORTIUM [Bacillus subtilis],1YIF_B CRYSTAL STRUCTURE OF beta-1,4-xylosidase FROM BACILLUS SUBTILIS, NEW YORK STRUCTURAL GENOMICS CONSORTIUM [Bacillus subtilis],1YIF_C CRYSTAL STRUCTURE OF beta-1,4-xylosidase FROM BACILLUS SUBTILIS, NEW YORK STRUCTURAL GENOMICS CONSORTIUM [Bacillus subtilis],1YIF_D CRYSTAL STRUCTURE OF beta-1,4-xylosidase FROM BACILLUS SUBTILIS, NEW YORK STRUCTURAL GENOMICS CONSORTIUM [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P94489 3.82e-182 1 537 1 532
Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynB PE=1 SV=2
P07129 2.67e-180 1 537 1 532
Beta-xylosidase OS=Bacillus pumilus OX=1408 GN=xynB PE=1 SV=2
P77713 1.01e-172 1 538 1 536
Putative beta-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yagH PE=3 SV=1
A9ZND1 4.07e-122 3 537 5 534
Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1
A7LXU0 1.07e-69 4 538 28 528
Non-reducing end alpha-L-arabinofuranosidase BoGH43B OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02656 PE=1 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
0.999930 0.000103 0.000001 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004860_01425.