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CAZyme Information: AO090003001291-T-p1

You are here: Home > Sequence: AO090003001291-T-p1

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 oryzae
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae
CAZyme ID AO090003001291-T-p1
CAZy Family AA7
CAZyme Description Ortholog(s) have rhamnogalacturonan acetylesterase activity and role in pectin catabolic process
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
663 71628.28 4.8278
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AoryzaeRIB40 12364 510516 274 12090
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 242 626 1.9e-71 0.7361111111111112

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
407469 Bac_rhamnosid6H 6.43e-08 180 447 3 237
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 0.002 316 419 359 459
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.
283786 GDE_C 0.005 258 427 31 220
Amylo-alpha-1,6-glucosidase. This family includes human glycogen branching enzyme AGL. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog GDB1 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 663 1 663
0.0 1 663 1 663
0.0 1 663 1 663
0.0 1 663 1 663
0.0 1 663 1 663

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.80e-08 70 583 194 658
Crystal structure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
1.49e-06 249 553 237 534
Chain A, Alpha-L-rhamnosidase [Klebsiella oxytoca],4XHC_B Chain B, Alpha-L-rhamnosidase [Klebsiella oxytoca]

Swiss-Prot Hits      help

AO090003001291-T-p1 has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.021499 0.978487 CS pos: 18-19. Pr: 0.6968

TMHMM  Annotations      help

There is no transmembrane helices in AO090003001291-T-p1.