Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q4WY82

- PPOC_ASPFU

UniProt

Q4WY82 - PPOC_ASPFU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
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.

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.
InParanoidiQ4WY82.
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

        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 .
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.
InParanoidi Q4WY82.
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

« 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: October 29, 2014
This is version 81 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