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CAZyme Information: EEU45321.1

You are here: Home > Sequence: EEU45321.1

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 Fusarium vanettenii
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium vanettenii
CAZyme ID EEU45321.1
CAZy Family GT1
CAZyme Description FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:C7YSZ5]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
580 64589.53 6.8413
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Fvanettenii77134 15708 660122 0 15708
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in EEU45321.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA4 34 565 1e-136 0.9865900383141762

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 7.75e-33 50 556 1 455
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 2.83e-28 86 225 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.
178402 PLN02805 3.58e-11 85 291 133 327
D-lactate dehydrogenase [cytochrome]
183043 PRK11230 5.56e-10 80 302 50 261
glycolate oxidase subunit GlcD; Provisional
273751 FAD_lactone_ox 0.004 86 222 15 147
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
8.03e-293 1 580 1 579
2.88e-271 9 568 8 570
9.89e-270 1 568 1 567
3.86e-252 9 542 8 544
4.41e-236 10 565 10 565

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.64e-103 35 564 5 522
Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXD_B Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXE_A Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXE_B Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXF_A Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXF_B Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXP_A Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1],5FXP_B Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1]
1.24e-89 35 565 6 528
Chain A, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBG_B Chain B, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_A Chain A, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_B Chain B, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_C Chain C, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_D Chain D, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_E Chain E, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_F Chain F, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_G Chain G, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_H Chain H, FAD-binding oxidoreductase [Gulosibacter chungangensis]
1.18e-87 35 566 12 556
Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1E0Y_B Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]
3.25e-87 35 566 12 556
Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]
4.56e-87 35 566 12 556
STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum],1W1K_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.48e-86 35 566 12 556
Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
2.00e-72 33 558 7 515
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
1.94e-16 38 300 26 275
Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1
4.37e-14 78 300 57 294
Probable D-lactate dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=LDHD PE=1 SV=1
4.73e-12 85 302 40 247
Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000053 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in EEU45321.1.