PPOA_EMENI
ID PPOA_EMENI Reviewed; 1081 AA.
AC G5EB19; C8VL39;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
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=AN1967;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 (By 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BN001307; CBF85912.1; -; Genomic_DNA.
DR EMBL; AACD01000029; EAA65132.1; -; Genomic_DNA.
DR RefSeq; XP_659571.1; XM_654479.1.
DR AlphaFoldDB; G5EB19; -.
DR SMR; G5EB19; -.
DR STRING; 162425.CADANIAP00008627; -.
DR EnsemblFungi; CBF85912; CBF85912; ANIA_01967.
DR EnsemblFungi; EAA65132; EAA65132; AN1967.2.
DR GeneID; 2875100; -.
DR KEGG; ani:AN1967.2; -.
DR VEuPathDB; FungiDB:AN1967; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_1_0_1; -.
DR InParanoid; G5EB19; -.
DR OMA; NEFRKYF; -.
DR OrthoDB; 276568at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IDA:AspGD.
DR GO; GO:0047888; F:fatty acid peroxidase 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; IDA:AspGD.
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:0043936; P:asexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:AspGD.
DR GO; GO:0043942; P:negative regulation of sexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IDA:AspGD.
DR GO; GO:0042316; P:penicillin metabolic process; IMP:AspGD.
DR GO; GO:0043945; P:positive regulation of asexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0043935; P:sexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0045461; P:sterigmatocystin biosynthetic process; IMP:AspGD.
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; Reference proteome.
FT CHAIN 1..1081
FT /note="Psi-producing oxygenase A"
FT /id="PRO_0000416226"
FT REGION 105..446
FT /note="Linoleate 8R-lipoxygenase"
FT /evidence="ECO:0000250"
FT REGION 654..1081
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 1081 AA; 120784 MW; 4F967A2E368C12B6 CRC64;
MGEDKETNIL AGLGNTISQV ENVVAASLRP LPTATGDGTY VAESTQTGLA KDLSHVDLKD
VRTLAEVVKS AATGEPVDDK QYIMERVIQL AAGLPSTSRN AAELTKSFLN MLWNDLEHPP
VSYLGADSMH RKADGSGNNR FWPQLGAAGS AYARSVRPKT MQSPSLPDPE TIFDCLLRRK
EYREHPNKIS SVLFYLASII IHDLFQTDPK DNSVSKTSSY LDLSPLYGNN QDEQNLVRTF
KDGKLKPDCF ATKRVLGFPP GVGVLLIMFN RFHNYVVDQL AAINECGRFT KPDESNVDEY
AKYDNNLFQT GRLVTCGLYA NIILKDYVRT ILNINRTDST WSLDPRMEMK DGLLGEAAAM
ATGNQVSAEF NVVYRWHACI SKRDEKWTED FHREIMPGVD PSTLSMQDFV AGLGRWQAGL
PQEPLERPFS GLQRKPDGAF NDDDLVNLFE KSVEDCAGAF GASHVPAIFK SVEALGIMQA
RRWNLGTLNE FRQYFNLAPH KTFEDINSDP YIADQLKRLY DHPDLVEIYP GVVVEEAKDS
MVPGSGLCTN FTISRAILSD AVALVRGDRF YTVDYTPKHL TNWAYNEIQP NNAVDQGQVF
YKLVLRAFPN HFDGNSIYAH FPLVVPSENE KILKSLGVAE KYSWEKPSRI SHPIFISSHA
ACMSILENQE TFKVTWGRKI EFLMQRDKHQ YGKDFMLSGD RPPNAASRKM MGSALYRDEW
EAEVKNFYEQ TTLKLLHKNS YKLAGVNQVD IVRDVANLAQ VHFCSSVFSL PLKTDSNPRG
IFAESELYKI MAAVFTAIFY DADIGKSFEL NQAARTVTQQ LGQLTMANVE IIAKTGLIAN
LVNRLHRRDV LSEYGIHMIQ RLLDSGLPAT EIVWTHILPT AGGMVANQAQ LFSQCLDYYL
SEEGSGHLPE INRLAKENTP EADELLTRYF MEGARLRSSV ALPRVAAQPT VVEDNGEKLT
IKAGQVVMCN LVSACMDPTA FPDPEKVKLD RDMNLYAHFG FGPHKCLGLD LCKTGLSTML
KVLGRLDNLR RAPGAQGQLK KLSGPGGIAK YMNEDQSGFT PFPSTMKIQW DGELPQLKED
F
