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CAZyme Information: ASPVEDRAFT_32615-t33_1-p1

You are here: Home > Sequence: ASPVEDRAFT_32615-t33_1-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 versicolor
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
CAZyme ID ASPVEDRAFT_32615-t33_1-p1
CAZy Family GH18
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
528 KV878134|CGC5 57788.02 4.5265
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AversicolorCBS583.65 13364 1036611 142 13222
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.-:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 59 272 9.8e-68 0.4650655021834061

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 4.72e-26 59 518 27 452
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 1.83e-25 64 199 1 139
FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
369658 BBE 2.40e-09 477 522 1 45
Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.
273751 FAD_lactone_ox 1.40e-07 75 227 26 177
sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
178402 PLN02805 3.10e-07 63 278 133 349
D-lactate dehydrogenase [cytochrome]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.48e-34 64 524 42 470
2.09e-33 63 525 62 488
2.86e-33 25 521 46 539
2.97e-33 13 521 16 489
1.07e-32 64 521 48 468

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.61e-41 40 522 24 469
Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
2.21e-41 40 522 24 469
Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
1.58e-32 35 521 8 469
Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale]
3.54e-31 58 521 37 476
The crystal structure of an Acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation [Sarocladium strictum],2AXR_A Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD [Sarocladium strictum]
5.48e-30 58 521 37 476
Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.04e-311 1 507 1 507
FAD-linked oxidoreductase pytB OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=pytB PE=2 SV=1
2.50e-216 5 527 15 538
FAD-linked oxidoreductase pynB OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=pynB PE=1 SV=1
8.01e-38 40 522 9 443
Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
3.25e-35 29 522 12 468
FAD-linked oxidoreductase sorD OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=sorD PE=3 SV=1
7.77e-32 1 521 1 491
Carbohydrate oxidase OS=Microdochium nivale OX=5520 GN=MnCO PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000220 0.999771 CS pos: 18-19. Pr: 0.9802

TMHMM  Annotations      help

There is no transmembrane helices in ASPVEDRAFT_32615-t33_1-p1.