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CAZyme Information: MGYG000002380_01156

You are here: Home > Sequence: MGYG000002380_01156

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 brevis
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Levilactobacillus; Levilactobacillus brevis
CAZyme ID MGYG000002380_01156
CAZy Family GH43
CAZyme Description Beta-xylosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
344 MGYG000002380_10|CGC2 38888.22 5.7454
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002380 2621559 Isolate Russia Europe
Gene Location Start: 24391;  End: 25425  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.37

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3507 XynB2 1.52e-45 1 334 236 547
Beta-xylosidase [Carbohydrate transport and metabolism].
pfam17851 GH43_C2 8.29e-40 132 334 3 203
Beta xylosidase C-terminal Concanavalin A-like domain. This domain is found to the C-terminus of the pfam04616 domain. This domain adopts a concanavalin A-like fold.
cd09000 GH43_SXA-like 3.11e-39 1 101 210 292
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 1.36e-20 2 94 200 272
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.
pfam04616 Glyco_hydro_43 2.72e-19 1 98 204 280
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
ABJ63538.1 3.59e-261 1 344 217 560
ARW21296.1 3.59e-261 1 344 217 560
QCZ45260.1 3.59e-261 1 344 217 560
ANN48319.1 2.67e-256 1 344 217 560
SQG75156.1 2.67e-256 1 344 217 560

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1YRZ_A 9.11e-43 1 334 216 524
ChainA, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125],1YRZ_B Chain B, xylan beta-1,4-xylosidase [Halalkalibacterium halodurans C-125]
6IFE_A 1.59e-39 1 340 232 552
AGlycoside Hydrolase Family 43 beta-Xylosidase [Bacillus pumilus],6IFE_B A Glycoside Hydrolase Family 43 beta-Xylosidase [Bacillus pumilus]
5ZQS_A 2.53e-38 1 331 214 528
Crystalstructure of beta-xylosidase mutant (E186Q/F503Y) from Bacillus pumilus [Bacillus pumilus],5ZQS_B Crystal structure of beta-xylosidase mutant (E186Q/F503Y) from Bacillus pumilus [Bacillus pumilus]
5ZQX_A 2.53e-38 1 331 214 528
Crystalstructure of beta-xylosidase mutant (E186Q) from Bacillus pumilus [Bacillus pumilus],5ZQX_B Crystal structure of beta-xylosidase mutant (E186Q) from Bacillus pumilus [Bacillus pumilus],5ZQX_C Crystal structure of beta-xylosidase mutant (E186Q) from Bacillus pumilus [Bacillus pumilus],5ZQX_D Crystal structure of beta-xylosidase mutant (E186Q) from Bacillus pumilus [Bacillus pumilus]
5ZQJ_A 2.53e-38 1 331 214 528
Crystalstructure of beta-xylosidase from Bacillus pumilus [Bacillus pumilus],5ZQJ_B Crystal structure of beta-xylosidase from Bacillus pumilus [Bacillus pumilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P07129 1.29e-37 1 331 214 528
Beta-xylosidase OS=Bacillus pumilus OX=1408 GN=xynB PE=1 SV=2
P77713 1.52e-34 3 334 216 534
Putative beta-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yagH PE=3 SV=1
P94489 1.75e-32 1 334 214 531
Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynB PE=1 SV=2
A9ZND1 3.04e-28 3 331 219 530
Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1
A7LXU0 1.41e-10 3 334 228 526
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
1.000083 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002380_01156.