ID   PPOA_ASPFC              Reviewed;        1079 AA.
AC   B0Y6R2;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Psi-producing oxygenase A;
DE   AltName: Full=Fatty acid oxygenase ppoA;
DE   Includes:
DE     RecName: Full=Linoleate 8R-lipoxygenase;
DE              EC=1.13.11.60;
DE   Includes:
DE     RecName: Full=9,12-octadecadienoate 8-hydroperoxide 8R-isomerase;
DE              EC=5.4.4.5;
GN   Name=ppoA; ORFNames=AFUB_067850;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Bifunctional heme-containing enzyme that oxidizes linoleic
CC       acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (within the N-
CC       terminal heme peroxidase domain), which is subsequently isomerized to
CC       (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (within the C-
CC       terminal P450 heme thiolate domain). Oxidized unsaturated fatty acids,
CC       so-called oxylipins, derived from endogenous fatty acids, influence the
CC       development of the asexual conidiophores and sexual cleistothecia and
CC       regulate the secondary metabolism. These substances were collectively
CC       named psi factors and are primarily a mixture of hydroxylated oleic,
CC       linoleic and alpha-linolenic acids. They are termed psi-beta, psi-
CC       alpha, and psi-gamma, respectively. Oxylipins may also serve as
CC       activators of mammalian immune responses contributing to enhanced
CC       resistance to opportunistic fungi and as factors that modulate fungal
CC       development contributing to resistance to host defenses (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + O2 = (8R,9Z,12Z)-8-
CC         hydroperoxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:25395,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:58659;
CC         EC=1.13.11.60;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate =
CC         (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate;
CC         Xref=Rhea:RHEA:31579, ChEBI:CHEBI:58659, ChEBI:CHEBI:63217;
CC         EC=5.4.4.5;
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00298}.
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DR   EMBL; DS499598; EDP50447.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y6R2; -.
DR   SMR; B0Y6R2; -.
DR   EnsemblFungi; EDP50447; EDP50447; AFUB_067850.
DR   VEuPathDB; FungiDB:AFUB_067850; -.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   PhylomeDB; B0Y6R2; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0052878; F:linoleate 8R-lipoxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd09817; linoleate_diol_synthase_like; 1.
DR   Gene3D; 1.10.630.10; -; 1.
DR   Gene3D; 1.10.640.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR034812; Ppo_N.
DR   Pfam; PF03098; An_peroxidase; 2.
DR   Pfam; PF00067; p450; 1.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Heme; Iron; Isomerase; Metal-binding; Multifunctional enzyme;
KW   Oxidoreductase; Peroxidase; Virulence.
FT   CHAIN           1..1079
FT                   /note="Psi-producing oxygenase A"
FT                   /id="PRO_0000416228"
FT   REGION          105..446
FT                   /note="Linoleate 8R-lipoxygenase"
FT                   /evidence="ECO:0000250"
FT   REGION          654..1079
FT                   /note="9,12-octadecadienoate 8-hydroperoxide 8R-isomerase"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000255"
FT   BINDING         202
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         377
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
SQ   SEQUENCE   1079 AA;  121192 MW;  EA5F6D04D426D5E7 CRC64;
     MSEKQTGSAN GGLGKTLAQL EQVVSASLRP LPSQTGDGTY VTEQVKTGIL KDLSHVDLGD
     LKTLVDVSKS ALTGEALDDR KYIMERVIQL SAGLPSTSQI GKELTNTFLT TLWNDLEHPP
     ISYLGRDAMY RRADGSGNNV LWPHIGAAGT PYARSVQPKT VQSPNLPDPE TLFDCLLARK
     EYKEHPNKIS SVLFYIASII IHDLFETDRK DPAISLTSSY LDLSPLYGNN QQEQDLIRTF
     KDGKLKPDCF STKRVLGFPP GVGVVLIMFN RFHNYVVEKL AMINEGGRFT KPQESDTAAY
     AKYDNDLFQT GRLVTCGLYV NIILKDYVRT ILNINRTDSI WSLDPRSEMK DGLLGRAAAQ
     ATGNQVAAEF NLVYRWHSCI SQRDQKWTED MYQELFPGQD PSKISLQDFL RGLGRWEAKL
     PGEPRERPFA GLQRKADGSY DDNDLVKIFE ESVEDCAGAF GALHVPTVFR SIEALGIQQA
     RSWNLATLNE FRKYFNLAPY KTFEEINSDP YVADQLKRLY DHPDRVEIYP GIIVEDAKES
     MAPGSGLCTN FTISRAILSD AVALVRGDRF HTVDFTPKHL TNWAYNEIQP QDSVDQTHVF
     YKLVLRAFPN HFRGDSIYAH FPLVVPSENK KILTKLGTAD KYSWDRPNYT PPPQFINSHS
     ACMSILSDQE TFKVTWGSKI EFLMRHNNQP YGRDFMLSGD RTPNAMSRQM MGKALYRDKW
     ETEVKRFYEN ITLKLLHRYS YKLAGVNQVD VVRDIANLAQ VHFCASVFSL PLKTESNPRG
     IFTESELYQI MAVVFTSIFY DADIGKSFEL NQAARAVTQQ LGQLTLANVE LIAKTGFIAN
     LVNSLHRHDV LSEYGVHMIQ RLLDSGMPAP EIVWTHVLPT AGGMVANQAQ LFSQSLDYYL
     SEEGSVHLPE INRLAKEDTT EADDLLLRYF MEGARIRSSV ALPRVVAQPT VVEDNGQKIT
     LKQGQHIICN LVSASMDPVT FPEPDKVKLD RDMNLYAHFG FGPHQCLGLG LCKTALTTML
     KVIGRLDNLR RAPGGQGKLK KLSGPGGIAM YMTPDQTAFF PFPTTMKIQW DGDLPEVKE