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CAZyme Information: KEF62899.1
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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 | Exophiala aquamarina | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala aquamarina | |||||||||||
| CAZyme ID | KEF62899.1 | |||||||||||
| CAZy Family | GT32 | |||||||||||
| CAZyme Description | FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A072PS26] | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| AA4 | 27 | 508 | 2e-121 | 0.9061302681992337 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 396238 | FAD_binding_4 | 5.97e-29 | 75 | 214 | 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. |
| 223354 | GlcD | 2.15e-23 | 44 | 272 | 2 | 221 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
| 178402 | PLN02805 | 3.32e-08 | 40 | 258 | 98 | 308 | D-lactate dehydrogenase [cytochrome] |
| 183043 | PRK11230 | 6.56e-08 | 75 | 259 | 56 | 232 | glycolate oxidase subunit GlcD; Provisional |
| 273751 | FAD_lactone_ox | 1.16e-05 | 75 | 211 | 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 |
|---|---|---|---|---|---|
| 3.22e-214 | 1 | 518 | 1 | 518 | |
| 5.05e-131 | 2 | 505 | 7 | 520 | |
| 7.17e-128 | 1 | 505 | 6 | 520 | |
| 1.89e-123 | 3 | 505 | 4 | 515 | |
| 4.31e-119 | 5 | 505 | 7 | 516 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 9.58e-89 | 28 | 513 | 5 | 486 | 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] |
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| 9.60e-71 | 28 | 521 | 12 | 530 | 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] |
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| 9.60e-71 | 28 | 521 | 12 | 530 | Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum] |
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| 1.29e-70 | 28 | 501 | 6 | 479 | 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] |
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| 2.62e-70 | 28 | 521 | 12 | 530 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1.35e-69 | 28 | 521 | 12 | 530 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
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| 7.87e-61 | 27 | 511 | 8 | 486 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
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| 6.40e-17 | 40 | 272 | 35 | 261 | Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1 |
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| 9.84e-17 | 40 | 285 | 6 | 244 | D-2-hydroxyglutarate dehydrogenase OS=Pseudomonas stutzeri (strain A1501) OX=379731 GN=d2hgdh PE=1 SV=1 |
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| 2.03e-15 | 41 | 284 | 32 | 290 | Probable D-lactate dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=LDHD PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000060 | 0.000001 |