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CAZyme Information: ASPBRDRAFT_116554-t33_1-p1

You are here: Home > Sequence: ASPBRDRAFT_116554-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 brasiliensis
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus brasiliensis
CAZyme ID ASPBRDRAFT_116554-t33_1-p1
CAZy Family AA1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
509 KV878680|CGC4 54995.87 5.0704
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AbrasiliensisCBS101740 13263 767769 274 12989
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in ASPBRDRAFT_116554-t33_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 71 498 7.7e-56 0.982532751091703

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 7.72e-23 83 497 32 450
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 6.35e-22 83 214 1 136
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.
215242 PLN02441 4.14e-10 83 240 65 233
cytokinin dehydrogenase
178402 PLN02805 1.24e-07 83 287 134 341
D-lactate dehydrogenase [cytochrome]
273751 FAD_lactone_ox 1.26e-05 83 254 15 187
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.68e-25 56 256 21 222
2.68e-25 56 256 21 222
8.93e-25 56 256 21 222
2.89e-24 64 273 19 233
1.16e-23 64 273 44 258

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.12e-25 64 273 25 239
Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
4.12e-25 64 273 25 239
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]
8.64e-23 59 241 22 204
The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
2.09e-22 59 241 22 204
The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
3.78e-22 59 241 22 204
The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.59e-77 47 509 31 509
FAD-dependent monooxygenase prx3 OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=prx3 PE=2 SV=1
2.17e-76 47 509 31 509
FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
2.17e-76 47 509 31 509
FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1
3.15e-55 61 507 56 517
FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
1.02e-53 59 507 57 524
FAD-dependent monooxygenase CTB5 OS=Cercospora beticola OX=122368 GN=CTB5 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000761 0.999218 CS pos: 16-17. Pr: 0.9544

TMHMM  Annotations      help

There is no transmembrane helices in ASPBRDRAFT_116554-t33_1-p1.