logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003367_00432

You are here: Home > Sequence: MGYG000003367_00432

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 sp007896885
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp007896885
CAZyme ID MGYG000003367_00432
CAZy Family GH143
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
623 70409.17 6.3829
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003367 3747359 MAG United States North America
Gene Location Start: 140808;  End: 142679  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003367_00432.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH143 23 574 1.5e-219 0.9910071942446043

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam13088 BNR_2 0.003 266 344 170 252
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
cd08989 GH43_XYL-like 0.007 63 120 52 113
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AXE18473.1 1.45e-279 1 613 2 621
AYQ36507.1 2.14e-279 2 613 3 622
AEI49119.1 6.41e-276 8 613 8 621
QJD77140.1 2.57e-275 3 616 2 614
QKZ12138.1 1.05e-274 10 614 9 621

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5MQS_A 6.00e-150 21 618 20 612
SialidaseBT_1020 [Bacteroides thetaiotaomicron]
5MQR_A 9.72e-148 21 618 20 612
SialidaseBT_1020 [Bacteroides thetaiotaomicron]

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.000267 0.999037 0.000220 0.000157 0.000156 0.000136

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003367_00432.