| IED ID | IndEnz0015000036 |
| Enzyme Type ID | laccase000036 |
| Protein Name |
FAD-linked oxidoreductase aurO EC 1.-.-.- Aurofusarin biosynthesis cluster protein O Gibberella pigment protein 3 |
| Gene Name | aurO GIP3 FG02321 FGRAMPH1_01T05587 |
| Organism | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Nectriaceae Fusarium Fusarium sambucinum species complex Gibberella zeae (Wheat head blight fungus) (Fusarium graminearum) Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
| Enzyme Sequence | MINSFSLFAHITPIIRSSLHSRYSVISSRKAMSSLAAAPYRHVMMPFSPAQDAQVHGNSALTKLTDAIPDLKIYTRSSPHYESLRGVYNKLITAQPLAICRPTSVAQVQAIVKTVSGLGIPLGVRGGGHDVFGRGCIADSVTIDMRELDTQELSQDKKTVKVGGGITSKNLVGFLGSHNLCTSNGFAGEAGWTSWASWGGYGPLGDYVGLGVDNIVGAKIVTASGDVVDAKGDSELLWALRGGGGNFGVIAETDVRVYPMSTIQAGFIVYPWPETADVLLRLQALLDSGVPDKLCLQAGFTKGEWGLGMAITYIWPEAETIGPESEEWLQKLKGLGTCIVDTVAETTFEAFQASISSAISNPVNVTSRHISISKFTSDTLNQLIGACESMPAEADCSITCTILHGKAAQANVLSAFGTRRPHIMLHINAVTEEAAHEHVAIAWADRLVDGVEATGDSIGSTYVSFMESDKDPKGCYGENWERLKAVKKEVDPNDVFRFVHGRIPAA |
| Enzyme Length | 506 |
| Uniprot Accession Number | I1RF55 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.-.-.- |
| Enzyme Function | FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin (PubMed:15811992, PubMed:15809006, PubMed:16879655). The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigment YWA1 (PubMed:21296881, PubMed:23557488). The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed during ring closure by an aldol-type cyclization reaction (PubMed:21296881). The dehydratase aurZ then acts as the first tailoring enzyme in the aurofusarin biosynthetic pathway by converting YWA1 to nor-rubrofusarin (PubMed:21296881, PubMed:23557488). Nor-rubrofusarin is then methylated to rubrofusarin by the O-methyltransferase aurJ (PubMed:21296881, PubMed:23557488). Rubrofusarin is then transported across the plasma membrane by the rubrofusarin-specific pump aurT for further enzymatic processing by the extracellular complex composed of GIP1, aurF, aurO and aurS to yield aurofusarin (PubMed:21296881). {ECO:0000269|PubMed:15809006, ECO:0000269|PubMed:15811992, ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:21296881, ECO:0000269|PubMed:23557488}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:15809006, ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:21296881}. |
| nucleotide Binding | |
| Features | Chain (1); Domain (1) |
| Keywords | FAD;Flavoprotein;Oxidoreductase;Reference proteome;Secreted |
| Interact With | |
| Induction | INDUCTION: Expression is regulated by the aurofusarin biosynthesis cluster-specific transcription factor aurR1/GIP2 (PubMed:16461721). {ECO:0000269|PubMed:16461721}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21296881}. Secreted, extracellular space {ECO:0000305|PubMed:21296881}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 54,117 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |