Detail Information for IndEnz0018001473
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