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CAZyme Information: PWY85103.1

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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 Aspergillus eucalypticola
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus eucalypticola
CAZyme ID PWY85103.1
CAZy Family GT4
CAZyme Description alpha-L-rhamnosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
655 70368.38 4.8961
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AeucalypticolaCBS122712 12207 1448314 274 11933
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 238 621 5.7e-75 0.7341269841269841

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
407469 Bac_rhamnosid6H 5.43e-13 175 509 3 302
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 2.62e-04 317 415 365 459
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.
379972 Bac_rhamnosid_C 0.007 559 621 1 63
Bacterial alpha-L-rhamnosidase C-terminal 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 655 1 655
0.0 1 655 1 655
0.0 1 655 1 655
0.0 1 654 1 654
0.0 1 654 1 654

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.05e-09 65 591 194 670
Crystal structure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits      help

PWY85103.1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000279 0.999696 CS pos: 17-18. Pr: 0.9615

TMHMM  Annotations      help

There is no transmembrane helices in PWY85103.1.