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Q4WY82

- PPOC_ASPFU

UniProt

Q4WY82 - PPOC_ASPFU

Protein

Linoleate 10R-lipoxygenase

Gene

ppoC

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
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    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

    1. dioxygenase activity Source: UniProtKB-KW
    2. heme binding Source: InterPro
    3. iron ion binding Source: InterPro
    4. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Source: InterPro
    5. peroxidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. hydrogen peroxide catabolic process Source: UniProtKB-KW
    2. prostaglandin biosynthetic process Source: ASPGD

    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.

    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-dioxygenaseImported1 Publication
    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: Chromosome 3

    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

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00004975.

    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.
    KOiK17862.
    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

    MLRRFSSTFK KKGDRESKQN GTASSSSAAV ANTNNNDNKR HSKISAARKS     50
    SSDDDRNEKK GNSVSPFEKY ASVLHASRSP IPNQTGDGAY LEHEHTTSLL 100
    QDARHLGFKD FKTLKEVIES KLPGGQLIDD KTMLMERIIQ LVSRLPHNSK 150
    HREELTNAFL TELWDSLPHP PLSYMGNDYA YRSADGSNNN PTLPRLGAAN 200
    TLYARTIPPL IIQPGGLPDP GLVFDTLFAR QTFKPHPNKV SSVFFYWASL 250
    IIHDIFQTDY KNPNMNKTSG YLDLSILYGD VQEEQNLIRT FKDGKLKPDS 300
    FSEPRLQAFP ATCCVLMVML NRFHNYAVEQ LAAINENGRF TKPADNLSEE 350
    EAKKAWAKYD EDLFQTGRLI TCGLYINITL YDYLRTIVNL NRTNSTWCLD 400
    PRAQMEGSHT APSGLGNQCS VEFNLAYRWH SATSATDEKW TEDVYERLMG 450
    KPASEVSMTE LLMGLGKYQA ELPKDPSKRT FADLERQADG RFKDEDLVNL 500
    LVNAVEDVAG SFGARNVPKV LKNVEILGII QSRKWNVGSL NEFRKFFGLK 550
    PYETFEEINS DPDVAESLRS LYDHPDFVEL YPGIVAEEAK QPMVPGVGIA 600
    PTYTISRAVL SDAVALVRGD RFYTIDYNPR NLTNWGYSEV RYDLSINQGC 650
    IFYKLATRAF PNWFKPDSIY AHYPMTIPSE NRKIMKDLGR EIHYSWDRPQ 700
    YTPPRVDLVS YSNAKLVAEQ QNQFRAAWGD TVEFVFGKAS KEFKLYQDSA 750
    FIQKHADVMS KLLNKEEWHR SVKEFYEDIT AKLLEDKTRR FGGINQVDIT 800
    NDVGNLTPVI FAANVFSLPL KSKENPRGIY TEHEMFKVLA ALYNCLYFDI 850
    DKTKSYPLHH ASQAVGEPLG KALEANVKAL GGSSLLSGIF RSFRENKNAL 900
    KEYGVHLTKQ LLENGLGAHE IAWAQFLPTV IAMVPAQAQA FTQIVDFYLS 950
    KEGSKHLPAI QRLAKQDTKK SDEQLLHYCL EAVRLNDMSG LYRQSETTLA 1000
    VTDEAVEVTI QPGDKVFVSF AKANRDASVF PDPAEVRLDR PMNSYINPTL 1050
    GPHGFLSKET SHIALTAMLR AVGRLNNLRV APGVQGQLKK IPQPGGYSAY 1100
    LREDHGSYSI FPTTFRVQYD A 1121
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ538183 mRNA. Translation: ACL14177.1 .
    AAHF01000002 Genomic DNA. Translation: EAL92371.2 .
    EU020168 mRNA. Translation: ABV21633.1 .
    RefSeqi XP_754409.2. XM_749316.2.

    3D structure databases

    ProteinModelPortali Q4WY82.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00004975.

    Protein family/group databases

    PeroxiBasei 5291. AfumLDS03.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00004975 ; CADAFUAP00004975 ; CADAFUAG00004975 .
    GeneIDi 3512584.
    KEGGi afm:AFUA_3G12120.

    Phylogenomic databases

    eggNOGi NOG39991.
    HOGENOMi HOG000190920.
    KOi K17862.
    OrthoDBi EOG7DNP3H.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-16944.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    1.10.640.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    [Graphical view ]
    Pfami PF03098. An_peroxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00457. ANPEROXIDASE.
    SUPFAMi SSF48113. SSF48113. 2 hits.
    SSF48264. SSF48264. 2 hits.
    PROSITEi PS50292. PEROXIDASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 80 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