ID   PPOA_ASPFU              Reviewed;        1079 AA.
AC   Q4WPX2; A7YMT1;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=AFUA_4G10770;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16040966; DOI=10.1128/iai.73.8.4548-4559.2005;
RA   Tsitsigiannis D.I., Bok J.W., Andes D., Nielsen K.F., Frisvad J.C.,
RA   Keller N.P.;
RT   "Aspergillus cyclooxygenase-like enzymes are associated with prostaglandin
RT   production and virulence.";
RL   Infect. Immun. 73:4548-4559(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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.
CC       {ECO:0000269|PubMed:16040966}.
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; EU020166; ABV21631.1; -; mRNA.
DR   EMBL; AAHF01000005; EAL89712.1; -; Genomic_DNA.
DR   RefSeq; XP_751750.1; XM_746657.1.
DR   AlphaFoldDB; Q4WPX2; -.
DR   SMR; Q4WPX2; -.
DR   STRING; 746128.CADAFUBP00006604; -.
DR   PeroxiBase; 5289; AfumLDS01.
DR   EnsemblFungi; EAL89712; EAL89712; AFUA_4G10770.
DR   GeneID; 3509289; -.
DR   KEGG; afm:AFUA_4G10770; -.
DR   VEuPathDB; FungiDB:Afu4g10770; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   InParanoid; Q4WPX2; -.
DR   OMA; NEFRKYF; -.
DR   OrthoDB; 276568at2759; -.
DR   PHI-base; PHI:494; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0051213; F:dioxygenase activity; IDA:AspGD.
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:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IMP:AspGD.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; IMP:AspGD.
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   2: Evidence at transcript level;
KW   Dioxygenase; Heme; Iron; Isomerase; Metal-binding; Multifunctional enzyme;
KW   Oxidoreductase; Peroxidase; Reference proteome; Virulence.
FT   CHAIN           1..1079
FT                   /note="Psi-producing oxygenase A"
FT                   /id="PRO_0000416227"
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;  121250 MW;  D6DFE2DD2A1CE77D 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 DVGVVLIMFN 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