Q4WY82 (PPOC_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Neosartorya fumigata

Protein attributes

Sequence length	1121 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Hydrogen peroxide Lipid biosynthesis Lipid metabolism Prostaglandin biosynthesis Prostaglandin metabolism
Ligand	Calcium Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase Peroxidase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW prostaglandin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1121	1121	Linoleate 10R-lipoxygenase		PRO_0000397942
Regions
	Compositional bias	24 – 27	4	Poly-Ser
Sites
	Active site	253	1	Proton acceptor By similarity
	Metal binding	254	1	Calcium By similarity
	Metal binding	269	1	Calcium By similarity
	Metal binding	271	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	273	1	Calcium By similarity
	Metal binding	275	1	Calcium By similarity
	Site	305	1	Transition state stabilizer By similarity
Experimental info
	Mutagenesis	306	1	L → A or V: Slightly lower synthesis of 8R-HODE. Little effect on epoxyalcohol synthase activity. Ref.1
	Mutagenesis	384	1	L → A: Increased synthesis of 8-HPODE, 8-HODE and altered product stereochemistry. Ref.1
	Mutagenesis	384	1	L → F: Increased synthesis of 8-HODE, synthesis of 9-HPODE and 13-HPODE. Retains chirality in 10- and 8-HODE. Ref.1
	Mutagenesis	384	1	L → M: Significantly increased synthesis of 8-HODE. Ref.1
	Mutagenesis	384	1	L → V: Increased synthesis of 8-HPODE and 8-HODE. Ref.1
	Mutagenesis	388	1	V → F: Increased synthesis of 8-HODE, synthesis of 9-HPODE and 13-HPODE. Retains chirality in 10- and 8-HODE. Ref.1
	Mutagenesis	388	1	V → L: Increased synthesis of 8-HODE. Ref.1
	Sequence conflict	237 – 253	17	PNKVS…SLIIH → MILKTSTRSVKDFNAKT in ABV21633. Ref.3
	Sequence conflict	323 – 331	9	FHNYAVEQL → SISNTN in ABV21633. Ref.3
	Sequence conflict	369	1	L → LLTNDS in ABV21633. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q4WY82 [UniParc]. Last modified April 17, 2007. Version 2. Checksum: AB09166AE6798232	FASTA	1,121	126,460
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
RefSeq	XP_754409.2. XM_749316.2.
3D structure databases
ProteinModelPortal	Q4WY82.
ModBase	Search...
Protein-protein interaction databases
STRING	5085.CADAFUAP00004975.
Protein family/group databases
PeroxiBase	5291. AfumLDS03.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00004975; CADAFUAP00004975; CADAFUAG00004975.
GeneID	3512584.
KEGG	afm:AFUA_3G12120.
Phylogenomic databases
eggNOG	NOG39991.
HOGENOM	HOG000190920.
KO	K11987.
OrthoDB	EOG4JDMFT.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16944.
Family and domain databases
Gene3D	1.10.630.10. 1 hit. 1.10.640.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR010255. Haem_peroxidase. IPR002007. Haem_peroxidase_animal. IPR019791. Haem_peroxidase_animal_subgr. [Graphical view]
Pfam	PF03098. An_peroxidase. 1 hit. [Graphical view]
PRINTS	PR00457. ANPEROXIDASE.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit. SSF48113. Peroxidase_super. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. False negative. PS00436. PEROXIDASE_2. False negative. PS50292. PEROXIDASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPOC_ASPFU

Accession

Primary (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:	May 1, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program