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Database: UniProt
Entry: A0A094DYZ1_9PEZI
LinkDB: A0A094DYZ1_9PEZI
Original site: A0A094DYZ1_9PEZI 
ID   A0A094DYZ1_9PEZI        Unreviewed;      1185 AA.
AC   A0A094DYZ1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Linoleate 8R-lipoxygenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V496_00222 {ECO:0000313|EMBL:KFY69453.1};
OS   Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY69453.1, ECO:0000313|Proteomes:UP000029302};
RN   [1] {ECO:0000313|EMBL:KFY69453.1, ECO:0000313|Proteomes:UP000029302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY69453.1}.
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DR   EMBL; JPJY01000037; KFY69453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094DYZ1; -.
DR   STRING; 1420909.A0A094DYZ1; -.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000029302; 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:0006631; P:fatty acid metabolic process; IEA:UniProt.
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:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR   Pfam; PF03098; An_peroxidase; 2.
DR   Pfam; PF00067; p450; 1.
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:UP000029302}.
FT   REGION          232..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         489
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   1185 AA;  131876 MW;  FB89DF6EC8903DCE CRC64;
     MSISHLHLAH VAQIAHDAPA ANLAKRPASL HIISTSRHRF TVPVTGTSRC LFRKPWFVCI
     CFRVRICIAA APPMQLPSPP RHPVTTSPAD LWSSPLLPPY LQWTPPPSPN QHGPQGAYSI
     PATPISQFKT LLGSIRRKPS HAPDGKTDEQ AYGKSMEEKT SILHDLTHLG VKNTKTVAEA
     ITTLASGEPM DDKDLLLEKG VSMLQSLPTN SGLSQTVSNN FIGMLWKDLP HPPPTTAGPT
     ARYRQPDGSG NNPWIPEMGK AGMPYSRSVP PMKPKGPNLP DPELVFDQLL KRTGPFREHP
     SGLNRLFFSF ATVVIHECFQ TSRTNPLINE TSSYVDLSTI YGNNAEEQKR VRTYEQGRIF
     PDSMASERIM MMPPGVVAVL LMFSRNHNHI VENLLTVNEG GKYKDWDSLD DEQKAWQDED
     LFQLTRNINV GFFATVVLKD YVAAILNTPR ANSHWSLDLG GEIKNGGERL ERGSGNVVSV
     EFAVLYHWHA ALSAADDQWM ESVIRKHIPD LQSIDDVTAA DFKKVMMTEG HQLMATPPKE
     WTFGGLQRGP DGKFNDVDLA EIIKDCIEEP AHAFGAHSTP ASLKIVDIMG QLQARDMFNV
     CTMNEFRRYL NLKPYEDFED WNPDKETARA AELLYGHIEN LELYPGLMAE VTKPAMPGSG
     VCPGHTTGRG ILDDAVALVR GDRFLSYDFN STTLSNWGVA KLGAIQAGAY GGMLPHLLFN
     ALPGAWTGTS TYALLPFYTP IAAKGILKGN KVLEQYDLER PASDKVVLGI HTHEGCKKVF
     EDRENFRVMY QAAIRKCTDG HDFLIGWDDA KRHDTRSSIL HKVFFEEGFE ANLQKFFRTN
     VSRLIKEKSL KYSNSRRSID IVRDVTNVTP ILWLAERFAI PLKTKETPHG LMSIPELFTI
     YLVLFMYQSF NIIPANEWKL REGAMKAAPA LRAVFEAHLK TQQGFKEGIV DWLAKGSSFE
     VGPDADRLYH ALNDSKLPIG DLVGDCIGMG APVAGNLTQQ ASLLIDLYLS EGYEEYKDRI
     IELSHKDDAA SERELQGFVF EGMRHAGVVP GLPRVASKDV TVMDGSRGPI NIKAGHTILI
     ATSKAAMDPI QFPNPEKLNP HRPFKDYILL GHGLHFCFGA RLVGCSLAAT LKEVFKLRNI
     RRANGRQGHF SIVEHEFAGV KMRQYLDSNA NESPIPTTLT LEYDE
//
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