PPOC_ASPFU
ID PPOC_ASPFU Reviewed; 1121 AA.
AC Q4WY82; A7YMT7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Linoleate 10R-lipoxygenase;
DE EC=1.13.11.62;
DE AltName: Full=Cyclooxygenase-like fatty acid oxygenase {ECO:0000312|EMBL:ABV21633.1};
DE AltName: Full=Fatty acid oxygenase ppoC {ECO:0000312|EMBL:EAL92371.2};
DE AltName: Full=Linoleate 10R-dioxygenase {ECO:0000303|PubMed:19289462, ECO:0000312|EMBL:ACL14177.1};
DE Short=10R-DOX {ECO:0000303|PubMed:19289462};
DE AltName: Full=Psi-producing oxygenase C {ECO:0000303|PubMed:16040966};
DE Short=AfPpoC {ECO:0000303|PubMed:16040966};
GN Name=ppoC {ECO:0000312|EMBL:ABV21633.1}; ORFNames=AFUA_3G12120;
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] {ECO:0000305, ECO:0000312|EMBL:ACL14177.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LEU-306; LEU-384 AND
RP VAL-388.
RX PubMed=19289462; DOI=10.1074/jbc.m808665200;
RA Garscha U., Oliw E.H.;
RT "Leucine/valine residues direct oxygenation of linoleic acid by (10R)- and
RT (8R)-dioxygenases: expression and site-directed mutagenesis of (10R)-
RT dioxygenase with epoxyalcohol synthase activity.";
RL J. Biol. Chem. 284:13755-13765(2009).
RN [2] {ECO:0000312|EMBL:EAL92371.2}
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).
RN [3] {ECO:0000305, ECO:0000312|EMBL:ABV21633.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 237-1121, FUNCTION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Responsible for the synthesis of various fatty acid-derived
CC oxylipins. Oxidizes linoleic acid primarily to 10R-hydroperoxy-8,12-
CC octadecadienoic acid (10R-HPODE) and, to a lesser extent, 8R-
CC hydroperoxylinoleic acid (8R-HPODE). Also synthesizes 10-hydroxy-
CC octadeca-8,12-dienoic acid (10-HODE) from linoleic acid and primarily
CC 8R-hydroxy-octadeca-9-monoenoic acid (8-HOME, also known as psiB beta)
CC from oleic acid. 8-HOME forms part of psi factor, a mixture of
CC oxylipins that regulates the balance between sexual and asexual spore
CC production. Displays epoxyalcohol synthase activity. Plays a role in
CC the synthesis of prostaglandins which may be required for
CC pathogenicity. {ECO:0000269|PubMed:16040966,
CC ECO:0000269|PubMed:19289462}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (8E,10R,12Z)-10-
CC hydroperoxyoctadeca-8,12-dienoate; Xref=Rhea:RHEA:31695,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:63324;
CC EC=1.13.11.62; Evidence={ECO:0000269|PubMed:19289462};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.05 mM for linoleic acid {ECO:0000269|PubMed:19289462};
CC -!- DISRUPTION PHENOTYPE: Decreased prostaglandin (PG) production in triple
CC ppoA/ppoB/ppoC mutants. The triple mutant is hypervirulent in the
CC invasive pulmonary aspergillosis murine model system and shows
CC increased tolerance to hydrogen peroxide stress.
CC {ECO:0000269|PubMed:16040966}.
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00298}.
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DR EMBL; FJ538183; ACL14177.1; -; mRNA.
DR EMBL; AAHF01000002; EAL92371.2; -; Genomic_DNA.
DR EMBL; EU020168; ABV21633.1; -; mRNA.
DR RefSeq; XP_754409.2; XM_749316.2.
DR AlphaFoldDB; Q4WY82; -.
DR SMR; Q4WY82; -.
DR STRING; 746128.CADAFUBP00003628; -.
DR PeroxiBase; 5291; AfumLDS03.
DR EnsemblFungi; EAL92371; EAL92371; AFUA_3G12120.
DR GeneID; 3512584; -.
DR KEGG; afm:AFUA_3G12120; -.
DR VEuPathDB; FungiDB:Afu3g12120; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_1_0_1; -.
DR InParanoid; Q4WY82; -.
DR OMA; YTIDYNP; -.
DR OrthoDB; 276568at2759; -.
DR BioCyc; MetaCyc:MON-16944; -.
DR BRENDA; 1.13.11.62; 508.
DR SABIO-RK; Q4WY82; -.
DR PHI-base; PHI:496; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
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; 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 PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW Calcium; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Hydrogen peroxide; Iron; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Peroxidase; Prostaglandin biosynthesis;
KW Prostaglandin metabolism; Reference proteome.
FT CHAIN 1..1121
FT /note="Linoleate 10R-lipoxygenase"
FT /id="PRO_0000397942"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 253
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT SITE 305
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT MUTAGEN 306
FT /note="L->A,V: Slightly lower synthesis of 8R-HODE. Little
FT effect on epoxyalcohol synthase activity."
FT /evidence="ECO:0000269|PubMed:19289462"
FT MUTAGEN 384
FT /note="L->A: Increased synthesis of 8-HPODE, 8-HODE and
FT altered product stereochemistry."
FT /evidence="ECO:0000269|PubMed:19289462"
FT MUTAGEN 384
FT /note="L->F: Increased synthesis of 8-HODE, synthesis of 9-
FT HPODE and 13-HPODE. Retains chirality in 10- and 8-HODE."
FT /evidence="ECO:0000269|PubMed:19289462"
FT MUTAGEN 384
FT /note="L->M: Significantly increased synthesis of 8-HODE."
FT /evidence="ECO:0000269|PubMed:19289462"
FT MUTAGEN 384
FT /note="L->V: Increased synthesis of 8-HPODE and 8-HODE."
FT /evidence="ECO:0000269|PubMed:19289462"
FT MUTAGEN 388
FT /note="V->F: Increased synthesis of 8-HODE, synthesis of 9-
FT HPODE and 13-HPODE. Retains chirality in 10- and 8-HODE."
FT /evidence="ECO:0000269|PubMed:19289462"
FT MUTAGEN 388
FT /note="V->L: Increased synthesis of 8-HODE."
FT /evidence="ECO:0000269|PubMed:19289462"
FT CONFLICT 237..253
FT /note="PNKVSSVFFYWASLIIH -> MILKTSTRSVKDFNAKT (in Ref. 3;
FT ABV21633)"
FT /evidence="ECO:0000305"
FT CONFLICT 323..331
FT /note="FHNYAVEQL -> SISNTN (in Ref. 3; ABV21633)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="L -> LLTNDS (in Ref. 3; ABV21633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1121 AA; 126460 MW; AB09166AE6798232 CRC64;
MLRRFSSTFK KKGDRESKQN GTASSSSAAV ANTNNNDNKR HSKISAARKS SSDDDRNEKK
GNSVSPFEKY ASVLHASRSP IPNQTGDGAY LEHEHTTSLL QDARHLGFKD FKTLKEVIES
KLPGGQLIDD KTMLMERIIQ LVSRLPHNSK HREELTNAFL TELWDSLPHP PLSYMGNDYA
YRSADGSNNN PTLPRLGAAN TLYARTIPPL IIQPGGLPDP GLVFDTLFAR QTFKPHPNKV
SSVFFYWASL IIHDIFQTDY KNPNMNKTSG YLDLSILYGD VQEEQNLIRT FKDGKLKPDS
FSEPRLQAFP ATCCVLMVML NRFHNYAVEQ LAAINENGRF TKPADNLSEE EAKKAWAKYD
EDLFQTGRLI TCGLYINITL YDYLRTIVNL NRTNSTWCLD PRAQMEGSHT APSGLGNQCS
VEFNLAYRWH SATSATDEKW TEDVYERLMG KPASEVSMTE LLMGLGKYQA ELPKDPSKRT
FADLERQADG RFKDEDLVNL LVNAVEDVAG SFGARNVPKV LKNVEILGII QSRKWNVGSL
NEFRKFFGLK PYETFEEINS DPDVAESLRS LYDHPDFVEL YPGIVAEEAK QPMVPGVGIA
PTYTISRAVL SDAVALVRGD RFYTIDYNPR NLTNWGYSEV RYDLSINQGC IFYKLATRAF
PNWFKPDSIY AHYPMTIPSE NRKIMKDLGR EIHYSWDRPQ YTPPRVDLVS YSNAKLVAEQ
QNQFRAAWGD TVEFVFGKAS KEFKLYQDSA FIQKHADVMS KLLNKEEWHR SVKEFYEDIT
AKLLEDKTRR FGGINQVDIT NDVGNLTPVI FAANVFSLPL KSKENPRGIY TEHEMFKVLA
ALYNCLYFDI DKTKSYPLHH ASQAVGEPLG KALEANVKAL GGSSLLSGIF RSFRENKNAL
KEYGVHLTKQ LLENGLGAHE IAWAQFLPTV IAMVPAQAQA FTQIVDFYLS KEGSKHLPAI
QRLAKQDTKK SDEQLLHYCL EAVRLNDMSG LYRQSETTLA VTDEAVEVTI QPGDKVFVSF
AKANRDASVF PDPAEVRLDR PMNSYINPTL GPHGFLSKET SHIALTAMLR AVGRLNNLRV
APGVQGQLKK IPQPGGYSAY LREDHGSYSI FPTTFRVQYD A
