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CAZyme Information: EGD95494.1

You are here: Home > Sequence: EGD95494.1

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 Trichophyton tonsurans
Lineage Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton tonsurans
CAZyme ID EGD95494.1
CAZy Family GH18
CAZyme Description glyoxal oxidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
852 92786.62 5.7670
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_TtonsuransCBS112818 8625 647933 104 8521
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in EGD95494.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA5 239 769 1.2e-153 0.9715808170515098

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
399910 Glyoxal_oxid_N 1.48e-47 253 499 1 243
Glyoxal oxidase N-terminus. This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium.
401164 DUF1929 7.42e-28 668 755 9 91
Domain of unknown function (DUF1929). Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. Their precise function, has not, as yet, been defined, though they are mostly found in sugar-utilising enzymes, such as galactose oxidase.
199882 E_set_GO_C 2.26e-24 652 755 5 103
C-terminal Early set domain associated with the catalytic domain of galactose oxidase. E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.
211316 ChtBD1_1 1.13e-14 178 217 1 39
Hevein or type 1 chitin binding domain; filamentous ascomycete subfamily. Hevein or type 1 chitin binding domain (ChtBD1), a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.
395135 Chitin_bind_1 7.01e-12 178 216 1 36
Chitin recognition protein.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.34e-274 174 756 46 628
6.62e-270 174 756 46 628
2.13e-262 167 755 243 826
1.46e-257 167 755 71 656
1.18e-256 167 755 232 817

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.79e-17 334 755 228 614
Structure of Galactose Oxidase homologue from Streptomyces lividans [Streptomyces lividans],4UNM_B Structure of Galactose Oxidase homologue from Streptomyces lividans [Streptomyces lividans]
3.71e-16 244 755 186 659
Chain A, GALACTOSE OXIDASE [Fusarium graminearum]
4.71e-16 244 755 164 637
Chain A, Galactose oxidase [Fusarium graminearum]
6.21e-16 244 755 164 637
Glactose oxidase C383S mutant identified by directed evolution [Fusarium sp.]
8.19e-16 244 755 164 637
NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE [Hypomyces rosellus],1GOG_A NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE [Hypomyces rosellus],1GOH_A NOVEL THIOETHER BOND REVEALED BY A 1.7 ANGSTROMS CRYSTAL STRUCTURE OF GALACTOSE OXIDASE [Hypomyces rosellus],2EIE_A Chain A, Galactose oxidase [Fusarium graminearum],2JKX_A Chain A, GALACTOSE OXIDASE [Fusarium graminearum],2VZ1_A Chain A, GALACTOSE OXIDASE [Fusarium graminearum],2VZ3_A Chain A, Galactose Oxidase [Fusarium graminearum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.11e-63 245 755 21 521
Aldehyde oxidase GLOX OS=Vitis pseudoreticulata OX=231512 GN=GLOX PE=2 SV=1
2.79e-62 247 755 104 614
Aldehyde oxidase GLOX1 OS=Arabidopsis thaliana OX=3702 GN=GLOX1 PE=2 SV=1
1.01e-52 260 765 440 914
WSC domain-containing protein ARB_07867 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07867 PE=1 SV=1
3.71e-49 247 756 76 594
Putative aldehyde oxidase Art an 7 OS=Artemisia annua OX=35608 PE=1 SV=1
5.62e-44 248 755 35 549
Aldehyde oxidase GLOX OS=Phanerodontia chrysosporium OX=2822231 GN=GLX PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000274 0.999687 CS pos: 15-16. Pr: 0.9606

TMHMM  Annotations      help

There is no transmembrane helices in EGD95494.1.