ID Q0ULH1_PHANO Unreviewed; 1108 AA.
AC Q0ULH1;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=Linoleate 8R-lipoxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_07393 {ECO:0000313|EMBL:EAT84859.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT84859.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; CH445335; EAT84859.1; -; Genomic_DNA.
DR RefSeq; XP_001797729.1; XM_001797677.1.
DR AlphaFoldDB; Q0ULH1; -.
DR PeroxiBase; 5343; PnoLDS01.
DR EnsemblFungi; SNOT_07393; SNOT_07393; SNOG_07393.
DR GeneID; 5974622; -.
DR KEGG; pno:SNOG_07393; -.
DR VEuPathDB; FungiDB:JI435_073930; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_1_0_1; -.
DR InParanoid; Q0ULH1; -.
DR OMA; KIQWDGD; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd20612; CYP_LDS-like_C; 1.
DR CDD; cd09817; linoleate_diol_synthase_like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR034812; Ppo-like_N.
DR PANTHER; PTHR11903:SF13; LINOLEATE 10R-LIPOXYGENASE; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 2.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT BINDING 417
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 1108 AA; 124272 MW; 4B961005AA3655AF CRC64;
MASDAKAAWD SHVDTRTGIT PPKPDEPSEL AKLRASVGSK FGAFAALMGA AAAPVPQTGD
GSKLAEEDPT VLKKIEGIMR DMSHLRIENM QTLLEAQKHK MTGELMDDKT YFMEGLIRTA
AALPDGSKTR DTVTHSFLEQ LWNDLEHPPQ SYLGAKYQYR SADGSNNSLK HPQLGAAGTP
YARTVKPSMM QTPARPDPGV VFDSIMTRKH AELHPNRISS MLFYLASIII HDCFRTSHED
YSVSMTSSYL DLSPLYGSNQ AEQDQMRTMI DGKIKPDCFS ESRLLFFPPG VGALLIMFNR
FHNYVVENLA LVNEQNRFPK PAAEAPKSTG DEEKDEAAKA KYEKSKVKYD NDLFQTGRLI
TCGLYVNIIL IDYVRTILDL NRTDSNWQLN PRAEMENVEL GVGNQVSAEF NLVYRWHSTV
SDRDEKWTQE MWDGLFGEGR DPKTVGKWEF LQRLNDVYKT TDPDPSKRKF AGLARNQDGT
LPDQELVDML VSSIEDCANS FGPNRVPSVF RAIEVLGIEQ ARSWNLGSLN EFRKHFDLEP
HKTFEDITSD KYVQEQLKHL YDHPDKVEIY PGIVVEDAKK PMAPGSGLCP GYTTSRAVLS
DAVALVRGDR FYTKDYNPST LTNWGYRCVD SDTDIDNGCV FYKLFLRAFP NHFKQNSVYA
HYPLTIPSAM QEALKDLKKD KLYDFSKPTP ASTLHVVKEY KLATQILLDQ STFKVAWGKA
MEFIMGPFGK EFSLAGDTPT NTASREMMSK ALYVKDWEKD VRAFYTSKTK ELLQEKSAHI
ADFNQVDIIR DVGNLAHVHF CAELFMLPLK TDERPHGIFT ESELYLILSS VFALIFFDVD
PAGSFPLHVK ARKATQVLGS VIEKNVEAIA HGGLLHAVTK AIWPEQGGLQ NYGIHMIQRL
LQTGMPAPQL VWGHIFGTAG AMVANQGQLF AQTLEYYILG EGKAHWASIQ ALAHDESESA
FAKLMHYAME GGRLNGETAV MRDVAQDSTT TTIRAGDRVF VDLRAASHDP NVFPNPDSVD
ITRPLDAYIH LGFGPHQCLG LPMVRVIMTA MLKEVAKLKN LRPAPGPQGK IHKVEKGVGE
EYPYHAYLTE MQDMYFPFPC SLKLVWDD
//