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CAZyme Information: CVK85001.1
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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 | Fusarium mangiferae | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium mangiferae | |||||||||||
| CAZyme ID | CVK85001.1 | |||||||||||
| CAZy Family | AA3 | |||||||||||
| CAZyme Description | FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A1L7SEP3] | |||||||||||
| CAZyme Property |
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| Genome Property |
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CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| AA7 | 23 | 233 | 3.8e-57 | 0.45414847161572053 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 223354 | GlcD | 3.61e-28 | 14 | 361 | 14 | 368 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
| 396238 | FAD_binding_4 | 9.04e-25 | 32 | 169 | 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. |
| 273751 | FAD_lactone_ox | 4.14e-09 | 6 | 218 | 9 | 198 | 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. |
| 273750 | pln_FAD_oxido | 2.48e-08 | 29 | 215 | 29 | 222 | plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown. |
| 215242 | PLN02441 | 2.86e-08 | 153 | 193 | 194 | 233 | cytokinin dehydrogenase |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 2.15e-24 | 30 | 203 | 18 | 191 | |
| 8.16e-21 | 21 | 229 | 154 | 352 | |
| 2.92e-20 | 15 | 203 | 32 | 218 | |
| 2.92e-20 | 15 | 203 | 32 | 218 | |
| 9.50e-20 | 15 | 203 | 32 | 218 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4.07e-15 | 20 | 289 | 44 | 307 | Crystal structure of tetrahydrocannabinolic acid synthase from Cannabis sativa [Cannabis sativa] |
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| 5.05e-15 | 23 | 198 | 53 | 226 | Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1] |
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| 9.14e-15 | 32 | 198 | 31 | 204 | Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_A Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6] |
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| 1.29e-14 | 5 | 197 | 40 | 230 | The Native Crystal Structure of the Primary Hexose Oxidase (Dbv29) in Antibiotic A40926 Biosynthesis [Nonomuraea gerenzanensis],2WDW_B The Native Crystal Structure of the Primary Hexose Oxidase (Dbv29) in Antibiotic A40926 Biosynthesis [Nonomuraea gerenzanensis],5AWV_A Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis],5AWV_B Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis],5AWV_C Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis],5AWV_D Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis] |
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| 2.69e-14 | 32 | 231 | 48 | 253 | Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3.55e-51 | 15 | 454 | 19 | 441 | FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1 |
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| 4.84e-51 | 9 | 454 | 16 | 442 | FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1 |
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| 2.08e-36 | 8 | 470 | 12 | 450 | FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1 |
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| 9.61e-35 | 8 | 470 | 12 | 450 | FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1 |
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| 1.20e-17 | 6 | 197 | 9 | 197 | Uncharacterized FAD-linked oxidoreductase YvdP OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdP PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000046 | 0.000000 |