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Q4WY82 (PPOC_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Linoleate 10R-lipoxygenase

EC=1.13.11.62
Alternative name(s):
Cyclooxygenase-like fatty acid oxygenase
Fatty acid oxygenase ppoC
Linoleate 10R-dioxygenase
Short name=10R-DOX
Psi-producing oxygenase C
Short name=AfPpoC
Gene names
Name:ppoC
ORF Names:AFUA_3G12120
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length1121 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.3

Catalytic activity

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

Disruption phenotype

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. Ref.3

Sequence similarities

Belongs to the peroxidase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.05 mM for linoleic acid Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11211121Linoleate 10R-lipoxygenase
PRO_0000397942

Regions

Compositional bias24 – 274Poly-Ser

Sites

Active site2531Proton acceptor By similarity
Metal binding2541Calcium By similarity
Metal binding2691Calcium By similarity
Metal binding2711Calcium; via carbonyl oxygen By similarity
Metal binding2731Calcium By similarity
Metal binding2751Calcium By similarity
Site3051Transition state stabilizer By similarity

Experimental info

Mutagenesis3061L → A or V: Slightly lower synthesis of 8R-HODE. Little effect on epoxyalcohol synthase activity. Ref.1
Mutagenesis3841L → A: Increased synthesis of 8-HPODE, 8-HODE and altered product stereochemistry. Ref.1
Mutagenesis3841L → F: Increased synthesis of 8-HODE, synthesis of 9-HPODE and 13-HPODE. Retains chirality in 10- and 8-HODE. Ref.1
Mutagenesis3841L → M: Significantly increased synthesis of 8-HODE. Ref.1
Mutagenesis3841L → V: Increased synthesis of 8-HPODE and 8-HODE. Ref.1
Mutagenesis3881V → F: Increased synthesis of 8-HODE, synthesis of 9-HPODE and 13-HPODE. Retains chirality in 10- and 8-HODE. Ref.1
Mutagenesis3881V → L: Increased synthesis of 8-HODE. Ref.1
Sequence conflict237 – 25317PNKVS…SLIIH → MILKTSTRSVKDFNAKT in ABV21633. Ref.3
Sequence conflict323 – 3319FHNYAVEQL → SISNTN in ABV21633. Ref.3
Sequence conflict3691L → LLTNDS in ABV21633. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q4WY82 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: AB09166AE6798232

FASTA1,121126,460
        10         20         30         40         50         60 
MLRRFSSTFK KKGDRESKQN GTASSSSAAV ANTNNNDNKR HSKISAARKS SSDDDRNEKK 

        70         80         90        100        110        120 
GNSVSPFEKY ASVLHASRSP IPNQTGDGAY LEHEHTTSLL QDARHLGFKD FKTLKEVIES 

       130        140        150        160        170        180 
KLPGGQLIDD KTMLMERIIQ LVSRLPHNSK HREELTNAFL TELWDSLPHP PLSYMGNDYA 

       190        200        210        220        230        240 
YRSADGSNNN PTLPRLGAAN TLYARTIPPL IIQPGGLPDP GLVFDTLFAR QTFKPHPNKV 

       250        260        270        280        290        300 
SSVFFYWASL IIHDIFQTDY KNPNMNKTSG YLDLSILYGD VQEEQNLIRT FKDGKLKPDS 

       310        320        330        340        350        360 
FSEPRLQAFP ATCCVLMVML NRFHNYAVEQ LAAINENGRF TKPADNLSEE EAKKAWAKYD 

       370        380        390        400        410        420 
EDLFQTGRLI TCGLYINITL YDYLRTIVNL NRTNSTWCLD PRAQMEGSHT APSGLGNQCS 

       430        440        450        460        470        480 
VEFNLAYRWH SATSATDEKW TEDVYERLMG KPASEVSMTE LLMGLGKYQA ELPKDPSKRT 

       490        500        510        520        530        540 
FADLERQADG RFKDEDLVNL LVNAVEDVAG SFGARNVPKV LKNVEILGII QSRKWNVGSL 

       550        560        570        580        590        600 
NEFRKFFGLK PYETFEEINS DPDVAESLRS LYDHPDFVEL YPGIVAEEAK QPMVPGVGIA 

       610        620        630        640        650        660 
PTYTISRAVL SDAVALVRGD RFYTIDYNPR NLTNWGYSEV RYDLSINQGC IFYKLATRAF 

       670        680        690        700        710        720 
PNWFKPDSIY AHYPMTIPSE NRKIMKDLGR EIHYSWDRPQ YTPPRVDLVS YSNAKLVAEQ 

       730        740        750        760        770        780 
QNQFRAAWGD TVEFVFGKAS KEFKLYQDSA FIQKHADVMS KLLNKEEWHR SVKEFYEDIT 

       790        800        810        820        830        840 
AKLLEDKTRR FGGINQVDIT NDVGNLTPVI FAANVFSLPL KSKENPRGIY TEHEMFKVLA 

       850        860        870        880        890        900 
ALYNCLYFDI DKTKSYPLHH ASQAVGEPLG KALEANVKAL GGSSLLSGIF RSFRENKNAL 

       910        920        930        940        950        960 
KEYGVHLTKQ LLENGLGAHE IAWAQFLPTV IAMVPAQAQA FTQIVDFYLS KEGSKHLPAI 

       970        980        990       1000       1010       1020 
QRLAKQDTKK SDEQLLHYCL EAVRLNDMSG LYRQSETTLA VTDEAVEVTI QPGDKVFVSF 

      1030       1040       1050       1060       1070       1080 
AKANRDASVF PDPAEVRLDR PMNSYINPTL GPHGFLSKET SHIALTAMLR AVGRLNNLRV 

      1090       1100       1110       1120 
APGVQGQLKK IPQPGGYSAY LREDHGSYSI FPTTFRVQYD A 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FJ538183 mRNA. Translation: ACL14177.1.
AAHF01000002 Genomic DNA. Translation: EAL92371.2.
EU020168 mRNA. Translation: ABV21633.1.
RefSeqXP_754409.2. XM_749316.2.

3D structure databases

ProteinModelPortalQ4WY82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00004975.

Protein family/group databases

PeroxiBase5291. AfumLDS03.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00004975; CADAFUAP00004975; CADAFUAG00004975.
GeneID3512584.
KEGGafm:AFUA_3G12120.

Phylogenomic databases

eggNOGNOG39991.
HOGENOMHOG000190920.
KOK17862.
OrthoDBEOG7DNP3H.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16944.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
1.10.640.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SUPFAMSSF48113. SSF48113. 2 hits.
SSF48264. SSF48264. 2 hits.
PROSITEPS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPOC_ASPFU
AccessionPrimary (citable) accession number: Q4WY82
Secondary accession number(s): A7YMT7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: April 17, 2007
Last modified: March 19, 2014
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families