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Database: UniProt/TrEMBL
Entry: Q0ULH1_PHANO
LinkDB: Q0ULH1_PHANO
Original site: Q0ULH1_PHANO 
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
//
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