ID PPOA_EMEND Reviewed; 1081 AA.
AC Q6RET3; Q5BBW3;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 120.
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;
OS Emericella nidulans (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=162425;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=14699095; DOI=10.1074/jbc.m310840200;
RA Tsitsigiannis D.I., Zarnowski R., Keller N.P.;
RT "The lipid body protein, PpoA, coordinates sexual and asexual sporulation
RT in Aspergillus nidulans.";
RL J. Biol. Chem. 279:11344-11353(2004).
RN [2]
RP SUBUNIT, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TYR-374 AND HIS-1004.
RX PubMed=19286665; DOI=10.1074/jbc.m809152200;
RA Brodhun F., Gobel C., Hornung E., Feussner I.;
RT "Identification of PpoA from Aspergillus nidulans as a fusion protein of a
RT fatty acid heme dioxygenase/peroxidase and a cytochrome P450.";
RL J. Biol. Chem. 284:11792-11805(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. {ECO:0000269|PubMed:14699095}.
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; Evidence={ECO:0000269|PubMed:19286665};
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; Evidence={ECO:0000269|PubMed:19286665};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:19286665};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for palmitoleic acid {ECO:0000269|PubMed:19286665};
CC KM=6.71 uM for oleic acid {ECO:0000269|PubMed:19286665};
CC KM=18.3 uM for linoleic acid {ECO:0000269|PubMed:19286665};
CC KM=22.6 uM for alpha-linolenic acid {ECO:0000269|PubMed:19286665};
CC Vmax=1.76 umol/min/mg enzyme toward palmitoleic acid
CC {ECO:0000269|PubMed:19286665};
CC Vmax=2.48 umol/min/mg enzyme toward oleic acid
CC {ECO:0000269|PubMed:19286665};
CC Vmax=3.16 umol/min/mg enzyme toward linoleic acid
CC {ECO:0000269|PubMed:19286665};
CC Vmax=2.97 umol/min/mg enzyme toward alpha-linolenic acid
CC {ECO:0000269|PubMed:19286665};
CC pH dependence:
CC Optimum pH is 7-7.5. {ECO:0000269|PubMed:19286665};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19286665}.
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00298}.
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DR EMBL; AY502073; AAR88626.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6RET3; -.
DR SASBDB; Q6RET3; -.
DR SMR; Q6RET3; -.
DR PeroxiBase; 5297; AniLDS01.
DR OMA; KIQWDGD; -.
DR BRENDA; 1.13.11.60; 517.
DR BRENDA; 5.4.4.5; 517.
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:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd20612; CYP_LDS-like_C; 1.
DR CDD; cd09817; linoleate_diol_synthase_like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 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-like_N.
DR PANTHER; PTHR11903:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 2.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Heme; Iron; Isomerase; Metal-binding; Multifunctional enzyme;
KW Oxidoreductase; Peroxidase.
FT CHAIN 1..1081
FT /note="Psi-producing oxygenase A"
FT /id="PRO_0000416225"
FT REGION 105..446
FT /note="Linoleate 8R-lipoxygenase"
FT REGION 654..1081
FT /note="9,12-octadecadienoate 8-hydroperoxide 8R-isomerase"
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"
FT MUTAGEN 374
FT /note="Y->F: Impairs the linoleate 8R-lipoxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:19286665"
FT MUTAGEN 1004
FT /note="H->A: Impairs the isomerase activity."
FT /evidence="ECO:0000269|PubMed:19286665"
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
//
