logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: EKG13088.1

You are here: Home > Sequence: EKG13088.1

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 Macrophomina phaseolina
Lineage Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
CAZyme ID EKG13088.1
CAZy Family CE16
CAZyme Description Bacterial alpha-L-rhamnosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
684 73588.64 4.2163
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_MphaseolinaMS6 14712 1126212 906 13806
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.40:5

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH78 246 631 1.1e-68 0.7341269841269841

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
407469 Bac_rhamnosid6H 1.91e-08 184 454 3 252
Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
273702 oligosac_amyl 1.25e-04 306 427 344 461
oligosaccharide amylase. The name of this type of amylase is based on the characterization of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterized glucoamylases, this T. vulgaris amylase hydrolyzes maltooligosaccharides (maltotetraose, maltose) more efficiently than starch (1), indicating this enzyme belongs to a class of glucoamylase-type enzymes with oligosaccharide-metabolizing activity.
183934 treF 0.001 379 433 349 403
alpha,alpha-trehalase TreF.
215307 PLN02567 0.002 382 433 331 382
alpha,alpha-trehalase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.04e-306 18 682 10 671
4.58e-305 16 682 12 674
2.57e-303 10 683 11 680
2.57e-303 10 683 11 680
1.58e-300 17 676 12 657

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.36e-15 146 589 272 658
Crystal structure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
6.18e-09 250 559 234 534
Chain A, Alpha-L-rhamnosidase [Klebsiella oxytoca],4XHC_B Chain B, Alpha-L-rhamnosidase [Klebsiella oxytoca]

Swiss-Prot Hits      help

EKG13088.1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000513 0.999453 CS pos: 23-24. Pr: 0.9782

TMHMM  Annotations      help

There is no transmembrane helices in EKG13088.1.