IED ID | IndEnz0018001473 |
Enzyme Type ID | peroxidase001473 |
Protein Name |
Psi-producing oxygenase A Fatty acid oxygenase ppoA Includes: Linoleate 8R-lipoxygenase EC 1.13.11.60 ; 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase EC 5.4.4.5 |
Gene Name | ppoA AFUA_4G10770 |
Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Enzyme Sequence | MSEKQTGSANGGLGKTLAQLEQVVSASLRPLPSQTGDGTYVTEQVKTGILKDLSHVDLGDLKTLVDVSKSALTGEALDDRKYIMERVIQLSAGLPSTSQIGKELTNTFLTTLWNDLEHPPISYLGRDAMYRRADGSGNNVLWPHIGAAGTPYARSVQPKTVQSPNLPDPETLFDCLLARKEYKEHPNKISSVLFYIASIIIHDLFETDRKDPAISLTSSYLDLSPLYGNNQQEQDLIRTFKDGKLKPDCFSTKRVLGFPPDVGVVLIMFNRFHNYVVEKLAMINEGGRFTKPQESDTAAYAKYDNDLFQTGRLVTCGLYVNIILKDYVRTILNINRTDSIWSLDPRSEMKDGLLGRAAAQATGNQVAAEFNLVYRWHSCISQRDQKWTEDMYQELFPGQDPSKISLQDFLRGLGRWEAKLPGEPRERPFAGLQRKADGSYDDNDLVKIFEESVEDCAGAFGALHVPTVFRSIEALGIQQARSWNLATLNEFRKYFNLAPYKTFEEINSDPYVADQLKRLYDHPDRVEIYPGIIVEDAKESMAPGSGLCTNFTISRAILSDAVALVRGDRFHTVDFTPKHLTNWAYNEIQPQDSVDQTHVFYKLVLRAFPNHFRGDSIYAHFPLVVPSENKKILTKLGTADKYSWDRPNYTPPPQFINSHSACMSILSDQETFKVTWGSKIEFLMRHNNQPYGRDFMLSGDRTPNAMSRQMMGKALYRDKWETEVKRFYENITLKLLHRYSYKLAGVNQVDVVRDIANLAQVHFCASVFSLPLKTESNPRGIFTESELYQIMAVVFTSIFYDADIGKSFELNQAARAVTQQLGQLTLANVELIAKTGFIANLVNSLHRHDVLSEYGVHMIQRLLDSGMPAPEIVWTHVLPTAGGMVANQAQLFSQSLDYYLSEEGSVHLPEINRLAKEDTTEADDLLLRYFMEGARIRSSVALPRVVAQPTVVEDNGQKITLKQGQHIICNLVSASMDPVTFPEPDKVKLDRDMNLYAHFGFGPHQCLGLGLCKTALTTMLKVIGRLDNLRRAPGGQGKLKKLSGPGGIAMYMTPDQTAFFPFPTTMKIQWDGDLPEVKE |
Enzyme Length | 1079 |
Uniprot Accession Number | Q4WPX2 |
Absorption | |
Active Site | ACT_SITE 374; /evidence=ECO:0000255 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:25395, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:58659; EC=1.13.11.60; CATALYTIC ACTIVITY: Reaction=(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate = (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:31579, ChEBI:CHEBI:58659, ChEBI:CHEBI:63217; EC=5.4.4.5; |
DNA Binding | |
EC Number | 1.13.11.60; 5.4.4.5 |
Enzyme Function | FUNCTION: Bifunctional heme-containing enzyme that oxidizes linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (within the N-terminal heme peroxidase domain), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (within the C-terminal P450 heme thiolate domain). Oxidized unsaturated fatty acids, so-called oxylipins, derived from endogenous fatty acids, influence the development of the asexual conidiophores and sexual cleistothecia and regulate the secondary metabolism. These substances were collectively named psi factors and are primarily a mixture of hydroxylated oleic, linoleic and alpha-linolenic acids. They are termed psi-beta, psi-alpha, and psi-gamma, respectively. Oxylipins may also serve as activators of mammalian immune responses contributing to enhanced resistance to opportunistic fungi and as factors that modulate fungal development contributing to resistance to host defenses. {ECO:0000269|PubMed:16040966}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Metal binding (2); Region (2) |
Keywords | Dioxygenase;Heme;Iron;Isomerase;Metal-binding;Multifunctional enzyme;Oxidoreductase;Peroxidase;Reference proteome;Virulence |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 121,250 |
Kinetics | |
Metal Binding | METAL 202; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298; METAL 377; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
Rhea ID | RHEA:25395; RHEA:31579 |
Cross Reference Brenda |