ID   C1GZP2_PARBA            Unreviewed;      1090 AA.
AC   C1GZP2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 2.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Linoleate diol synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PAAG_03986 {ECO:0000313|EMBL:EEH42065.2};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH42065.2, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:EEH42065.2, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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DR   EMBL; KN294000; EEH42065.2; -; Genomic_DNA.
DR   RefSeq; XP_015702212.1; XM_015845123.1.
DR   AlphaFoldDB; C1GZP2; -.
DR   STRING; 502779.C1GZP2; -.
DR   GeneID; 9097470; -.
DR   KEGG; pbl:PAAG_03986; -.
DR   VEuPathDB; FungiDB:PAAG_03986; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   OMA; RHYTIDY; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000002059; Partially assembled 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; 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   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:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002059}.
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         403
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   1090 AA;  123126 MW;  528A7DF941542DAB CRC64;
     MASGSEAVGA SSHDKRNGQM NGKPKTSSPP WAKRSNGRCI KRQEVERTFA KYAEFSGDFT
     QAKKAVSNGI FKEVKWMGLK GIRTLLAVVK SKTSGTLTDD KEYLMERIIQ LVASLPPEST
     ARVKLTNSFV KSLWISLPHP PLSYLGDEYR YRAADGSNNN PLFPRLGAAN TAYARSIKPS
     TIQPAALPDP GLVFDSLFAR QEFKPHPNGV SSMFFNWASL IIHDLFETDP RNQHISLTSS
     YLDLSTLYGD NQQQQDDMRT FRDGKLKPDT FADPRLIALP PGCSVILVLL NRFHNYVVEQ
     LAHINENGRF TKPRDDLASE ESRNAWAKYD NDLFQTGRLI TCGLYINITL YDYVRTIINL
     TRTNTNWSLD PRVNMKKGAK PEAAESGVGN QVSFEFNLAY RWHSTIGEID EKWIEEIYLD
     LFGKTAEEIS MEELMAGMGK WKRNLPKDPA QRTFAKLERQ ADGRFKDEDL VRIITEATEE
     VAGTFGPRNV PKALRAVEIL GIHQARKFGC GSLNEFRKFF GLKEYETFEE INSDPIIAHQ
     LRSLYEHPDY VELYPGIVSE EAKIPMVPGA GICPTYTISR AVLSDAVALV RGDRFYTTDY
     NAKNLTNWGY AESHYDLSVN QGCMFYKLML RALPNYIKPD SIYAHYPMTI PSVNREIFTK
     LGRESHFSWD RPALIPPRID LTSYNGTKTI LENVRDFRFT FGDAATSLFG SQSFNVSQSE
     ILDETFRQDS WRQNVKKFYE DITLNLLRQN SVRVAGINQI DITRDVGNLA HVYFAASTFD
     LPLKTKENPK GLFTDREMFM VIVAIFTSVF FDVDPTKSFA LRQVTREAGE ELGKVVESYV
     KSAKGFTYLS GIFDRFQKHD NPLAKYGLDA TRKLLKCGLS VSEVAWSQLL PIICTAVPSQ
     AQVFTQIIDF YLSDEGKTHL PEINRLAHED SPESDAKLLH YCMEGIRLNG TFKSYREANT
     NVLINDTGRD VVVNDGDKVF VSMISSSRDP NIFPSPDDVV LDRPLESYIH FTDSAFTCFG
     RGAHMVALTS MLRVVGRLDN LRAAPGPQGR LVKVTRPNGH FAYMREDYGS YSVLPMTLKV
     HYDGVLPESI
//