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Protein

Linoleate 10R-lipoxygenase

Gene

ppoC

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for the synthesis of various fatty acid-derived oxylipins. Oxidizes linoleic acid primarily to 10R-hydroperoxy-8,12-octadecadienoic acid (10R-HPODE) and, to a lesser extent, 8R-hydroperoxylinoleic acid (8R-HPODE). Also synthesizes 10-hydroxy-octadeca-8,12-dienoic acid (10-HODE) from linoleic acid and primarily 8R-hydroxy-octadeca-9-monoenoic acid (8-HOME, also known as psiB beta) from oleic acid. 8-HOME forms part of psi factor, a mixture of oxylipins that regulates the balance between sexual and asexual spore production. Displays epoxyalcohol synthase activity. Plays a role in the synthesis of prostaglandins which may be required for pathogenicity.2 Publications

Catalytic activityi

Linoleate + O2 = (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate.1 Publication

Kineticsi

  1. KM=0.05 mM for linoleic acid1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei253 – 2531Proton acceptorPROSITE-ProRule annotation
    Metal bindingi254 – 2541CalciumPROSITE-ProRule annotation
    Metal bindingi269 – 2691CalciumPROSITE-ProRule annotation
    Metal bindingi271 – 2711Calcium; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi273 – 2731CalciumPROSITE-ProRule annotation
    Metal bindingi275 – 2751CalciumPROSITE-ProRule annotation
    Sitei305 – 3051Transition state stabilizerPROSITE-ProRule annotation

    GO - Molecular functioni

    GO - Biological processi

    • hydrogen peroxide catabolic process Source: UniProtKB-KW
    • prostaglandin biosynthetic process Source: ASPGD
    • response to oxidative stress Source: InterPro
    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Hydrogen peroxide, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

    Keywords - Ligandi

    Calcium, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16944.
    BRENDAi1.13.11.62. 508.

    Protein family/group databases

    PeroxiBasei5291. AfumLDS03.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Linoleate 10R-lipoxygenase (EC:1.13.11.62)
    Alternative name(s):
    Cyclooxygenase-like fatty acid oxygenaseImported
    Fatty acid oxygenase ppoCImported
    Linoleate 10R-dioxygenase1 PublicationImported
    Short name:
    10R-DOX1 Publication
    Psi-producing oxygenase C1 Publication
    Short name:
    AfPpoC1 Publication
    Gene namesi
    Name:ppoCImported
    ORF Names:AFUA_3G12120
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530 Componenti: Chromosome 3

    Organism-specific databases

    EuPathDBiFungiDB:Afu3g12120.

    Pathology & Biotechi

    Disruption phenotypei

    Decreased prostaglandin (PG) production in triple ppoA/ppoB/ppoC mutants. The triple mutant is hypervirulent in the invasive pulmonary aspergillosis murine model system and shows increased tolerance to hydrogen peroxide stress.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi306 – 3061L → A or V: Slightly lower synthesis of 8R-HODE. Little effect on epoxyalcohol synthase activity. 1 Publication
    Mutagenesisi384 – 3841L → A: Increased synthesis of 8-HPODE, 8-HODE and altered product stereochemistry. 1 Publication
    Mutagenesisi384 – 3841L → F: Increased synthesis of 8-HODE, synthesis of 9-HPODE and 13-HPODE. Retains chirality in 10- and 8-HODE. 1 Publication
    Mutagenesisi384 – 3841L → M: Significantly increased synthesis of 8-HODE. 1 Publication
    Mutagenesisi384 – 3841L → V: Increased synthesis of 8-HPODE and 8-HODE. 1 Publication
    Mutagenesisi388 – 3881V → F: Increased synthesis of 8-HODE, synthesis of 9-HPODE and 13-HPODE. Retains chirality in 10- and 8-HODE. 1 Publication
    Mutagenesisi388 – 3881V → L: Increased synthesis of 8-HODE. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11211121Linoleate 10R-lipoxygenasePRO_0000397942Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WY82.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi24 – 274Poly-SerSequence Analysis

    Sequence similaritiesi

    Belongs to the peroxidase family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG39991.
    HOGENOMiHOG000190920.
    InParanoidiQ4WY82.
    KOiK17862.
    OMAiSMKVTWD.
    OrthoDBiEOG7DNP3H.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    1.10.640.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    [Graphical view]
    PfamiPF03098. An_peroxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00457. ANPEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 2 hits.
    SSF48264. SSF48264. 2 hits.
    PROSITEiPS50292. PEROXIDASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q4WY82-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLRRFSSTFK KKGDRESKQN GTASSSSAAV ANTNNNDNKR HSKISAARKS
    60 70 80 90 100
    SSDDDRNEKK GNSVSPFEKY ASVLHASRSP IPNQTGDGAY LEHEHTTSLL
    110 120 130 140 150
    QDARHLGFKD FKTLKEVIES KLPGGQLIDD KTMLMERIIQ LVSRLPHNSK
    160 170 180 190 200
    HREELTNAFL TELWDSLPHP PLSYMGNDYA YRSADGSNNN PTLPRLGAAN
    210 220 230 240 250
    TLYARTIPPL IIQPGGLPDP GLVFDTLFAR QTFKPHPNKV SSVFFYWASL
    260 270 280 290 300
    IIHDIFQTDY KNPNMNKTSG YLDLSILYGD VQEEQNLIRT FKDGKLKPDS
    310 320 330 340 350
    FSEPRLQAFP ATCCVLMVML NRFHNYAVEQ LAAINENGRF TKPADNLSEE
    360 370 380 390 400
    EAKKAWAKYD EDLFQTGRLI TCGLYINITL YDYLRTIVNL NRTNSTWCLD
    410 420 430 440 450
    PRAQMEGSHT APSGLGNQCS VEFNLAYRWH SATSATDEKW TEDVYERLMG
    460 470 480 490 500
    KPASEVSMTE LLMGLGKYQA ELPKDPSKRT FADLERQADG RFKDEDLVNL
    510 520 530 540 550
    LVNAVEDVAG SFGARNVPKV LKNVEILGII QSRKWNVGSL NEFRKFFGLK
    560 570 580 590 600
    PYETFEEINS DPDVAESLRS LYDHPDFVEL YPGIVAEEAK QPMVPGVGIA
    610 620 630 640 650
    PTYTISRAVL SDAVALVRGD RFYTIDYNPR NLTNWGYSEV RYDLSINQGC
    660 670 680 690 700
    IFYKLATRAF PNWFKPDSIY AHYPMTIPSE NRKIMKDLGR EIHYSWDRPQ
    710 720 730 740 750
    YTPPRVDLVS YSNAKLVAEQ QNQFRAAWGD TVEFVFGKAS KEFKLYQDSA
    760 770 780 790 800
    FIQKHADVMS KLLNKEEWHR SVKEFYEDIT AKLLEDKTRR FGGINQVDIT
    810 820 830 840 850
    NDVGNLTPVI FAANVFSLPL KSKENPRGIY TEHEMFKVLA ALYNCLYFDI
    860 870 880 890 900
    DKTKSYPLHH ASQAVGEPLG KALEANVKAL GGSSLLSGIF RSFRENKNAL
    910 920 930 940 950
    KEYGVHLTKQ LLENGLGAHE IAWAQFLPTV IAMVPAQAQA FTQIVDFYLS
    960 970 980 990 1000
    KEGSKHLPAI QRLAKQDTKK SDEQLLHYCL EAVRLNDMSG LYRQSETTLA
    1010 1020 1030 1040 1050
    VTDEAVEVTI QPGDKVFVSF AKANRDASVF PDPAEVRLDR PMNSYINPTL
    1060 1070 1080 1090 1100
    GPHGFLSKET SHIALTAMLR AVGRLNNLRV APGVQGQLKK IPQPGGYSAY
    1110 1120
    LREDHGSYSI FPTTFRVQYD A
    Length:1,121
    Mass (Da):126,460
    Last modified:April 17, 2007 - v2
    Checksum:iAB09166AE6798232
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti237 – 25317PNKVS…SLIIH → MILKTSTRSVKDFNAKT in ABV21633 (PubMed:16040966).CuratedAdd
    BLAST
    Sequence conflicti323 – 3319FHNYAVEQL → SISNTN in ABV21633 (PubMed:16040966).Curated
    Sequence conflicti369 – 3691L → LLTNDS in ABV21633 (PubMed:16040966).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    FJ538183 mRNA. Translation: ACL14177.1.
    AAHF01000002 Genomic DNA. Translation: EAL92371.2.
    EU020168 mRNA. Translation: ABV21633.1.
    RefSeqiXP_754409.2. XM_749316.2.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00004975; CADAFUAP00004975; CADAFUAG00004975.
    GeneIDi3512584.
    KEGGiafm:AFUA_3G12120.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    FJ538183 mRNA. Translation: ACL14177.1.
    AAHF01000002 Genomic DNA. Translation: EAL92371.2.
    EU020168 mRNA. Translation: ABV21633.1.
    RefSeqiXP_754409.2. XM_749316.2.

    3D structure databases

    ProteinModelPortaliQ4WY82.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    PeroxiBasei5291. AfumLDS03.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiCADAFUAT00004975; CADAFUAP00004975; CADAFUAG00004975.
    GeneIDi3512584.
    KEGGiafm:AFUA_3G12120.

    Organism-specific databases

    EuPathDBiFungiDB:Afu3g12120.

    Phylogenomic databases

    eggNOGiNOG39991.
    HOGENOMiHOG000190920.
    InParanoidiQ4WY82.
    KOiK17862.
    OMAiSMKVTWD.
    OrthoDBiEOG7DNP3H.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16944.
    BRENDAi1.13.11.62. 508.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    1.10.640.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    [Graphical view]
    PfamiPF03098. An_peroxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00457. ANPEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 2 hits.
    SSF48264. SSF48264. 2 hits.
    PROSITEiPS50292. PEROXIDASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Leucine/valine residues direct oxygenation of linoleic acid by (10R)- and (8R)-dioxygenases: expression and site-directed mutagenesis of (10R)-dioxygenase with epoxyalcohol synthase activity."
      Garscha U., Oliw E.H.
      J. Biol. Chem. 284:13755-13765(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LEU-306; LEU-384 AND VAL-388.
    2. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
      Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
      , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
      Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
    3. "Aspergillus cyclooxygenase-like enzymes are associated with prostaglandin production and virulence."
      Tsitsigiannis D.I., Bok J.W., Andes D., Nielsen K.F., Frisvad J.C., Keller N.P.
      Infect. Immun. 73:4548-4559(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 237-1121, FUNCTION, DISRUPTION PHENOTYPE.
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

    Entry informationi

    Entry nameiPPOC_ASPFU
    AccessioniPrimary (citable) accession number: Q4WY82
    Secondary accession number(s): A7YMT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: April 17, 2007
    Last modified: June 24, 2015
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.