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CAZyme Information: PWY64605.1

You are here: Home > Sequence: PWY64605.1

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 Aspergillus eucalypticola
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus eucalypticola
CAZyme ID PWY64605.1
CAZy Family AA7
CAZyme Description FAD binding domain protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
509 55129.06 5.2156
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

No EC number prediction in PWY64605.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 73 498 8.4e-57 0.9781659388646288

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 8.17e-26 83 497 32 450
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 1.12e-21 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 7.74e-09 83 240 65 233
cytokinin dehydrogenase
178402 PLN02805 3.86e-07 83 287 134 341
D-lactate dehydrogenase [cytochrome]
273751 FAD_lactone_ox 8.65e-06 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
4.38e-26 56 256 21 222
4.38e-26 56 256 21 222
1.47e-25 56 256 21 222
2.14e-24 75 273 29 233
1.56e-23 75 273 54 258

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.54e-25 75 273 35 239
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]
5.54e-25 75 273 35 239
Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
6.43e-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]
1.56e-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]
2.81e-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
2.84e-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
1.26e-74 47 509 31 509
FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
1.26e-74 47 509 31 509
FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1
1.41e-54 57 507 55 524
FAD-dependent monooxygenase CTB5 OS=Cercospora beticola OX=122368 GN=CTB5 PE=3 SV=1
2.15e-54 43 507 54 514
Bifunctional solanapyrone synthase OS=Alternaria solani OX=48100 GN=sol5 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000327 0.999665 CS pos: 25-26. Pr: 0.9002

TMHMM  Annotations      help

There is no transmembrane helices in PWY64605.1.