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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: -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)DescriptionActionsGraphical viewLength
    Active sitei253Proton acceptorPROSITE-ProRule annotation1
    Metal bindingi254CalciumPROSITE-ProRule annotation1
    Metal bindingi269CalciumPROSITE-ProRule annotation1
    Metal bindingi271Calcium; via carbonyl oxygenPROSITE-ProRule annotation1
    Metal bindingi273CalciumPROSITE-ProRule annotation1
    Metal bindingi275CalciumPROSITE-ProRule annotation1
    Sitei305Transition state stabilizerPROSITE-ProRule annotation1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionDioxygenase, Oxidoreductase, Peroxidase
    Biological processFatty acid biosynthesis, Fatty acid metabolism, Hydrogen peroxide, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism
    LigandCalcium, 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
    Proteomesi
    • UP000002530 Componentsi: Chromosome 3, Unassembled WGS sequence

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi306L → A or V: Slightly lower synthesis of 8R-HODE. Little effect on epoxyalcohol synthase activity. 1 Publication1
    Mutagenesisi384L → A: Increased synthesis of 8-HPODE, 8-HODE and altered product stereochemistry. 1 Publication1
    Mutagenesisi384L → F: Increased synthesis of 8-HODE, synthesis of 9-HPODE and 13-HPODE. Retains chirality in 10- and 8-HODE. 1 Publication1
    Mutagenesisi384L → M: Significantly increased synthesis of 8-HODE. 1 Publication1
    Mutagenesisi384L → V: Increased synthesis of 8-HPODE and 8-HODE. 1 Publication1
    Mutagenesisi388V → F: Increased synthesis of 8-HODE, synthesis of 9-HPODE and 13-HPODE. Retains chirality in 10- and 8-HODE. 1 Publication1
    Mutagenesisi388V → L: Increased synthesis of 8-HODE. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003979421 – 1121Linoleate 10R-lipoxygenaseAdd BLAST1121

    Proteomic databases

    PRIDEiQ4WY82

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUBP00003628

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WY82
    SMRiQ4WY82
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Compositional biasi24 – 27Poly-SerSequence analysis4

    Sequence similaritiesi

    Belongs to the peroxidase family.PROSITE-ProRule annotation

    Phylogenomic databases

    HOGENOMiHOG000190920
    InParanoidiQ4WY82
    KOiK17862
    OMAiVYAHYPM
    OrthoDBiEOG092C0D86

    Family and domain databases

    CDDicd09817 linoleate_diol_synthase_like, 1 hit
    Gene3Di1.10.640.10, 1 hit
    InterProiView protein in InterPro
    IPR036396 Cyt_P450_sf
    IPR010255 Haem_peroxidase
    IPR019791 Haem_peroxidase_animal
    IPR037120 Haem_peroxidase_sf
    IPR034807 Ppo
    IPR034812 Ppo_N
    PANTHERiPTHR11903:SF13 PTHR11903:SF13, 1 hit
    PfamiView protein in Pfam
    PF03098 An_peroxidase, 2 hits
    PRINTSiPR00457 ANPEROXIDASE
    SUPFAMiSSF48113 SSF48113, 2 hits
    SSF48264 SSF48264, 2 hits
    PROSITEiView protein in PROSITE
    PS50292 PEROXIDASE_3, 1 hit

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti237 – 253PNKVS…SLIIH → MILKTSTRSVKDFNAKT in ABV21633 (PubMed:16040966).CuratedAdd BLAST17
    Sequence conflicti323 – 331FHNYAVEQL → SISNTN in ABV21633 (PubMed:16040966).Curated9
    Sequence conflicti369L → LLTNDS in ABV21633 (PubMed:16040966).Curated1

    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

    Similar proteinsi

    Entry informationi

    Entry nameiPPOC_ASPFU
    AccessioniPrimary (citable) accession number: Q4WY82
    Secondary accession number(s): A7YMT7
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: April 17, 2007
    Last modified: May 23, 2018
    This is version 103 of the entry and version 2 of the sequence. See 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

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