ID C1G5A2_PARBD Unreviewed; 1066 AA.
AC C1G5A2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Linoleate 8R-lipoxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PADG_03472 {ECO:0000313|EMBL:EEH47374.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH47374.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH47374.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH47374.2,
RC ECO:0000313|Proteomes:UP000001628};
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; KN275959; EEH47374.2; -; Genomic_DNA.
DR RefSeq; XP_010758416.1; XM_010760114.1.
DR AlphaFoldDB; C1G5A2; -.
DR STRING; 502780.C1G5A2; -.
DR GeneID; 22582771; -.
DR KEGG; pbn:PADG_03472; -.
DR VEuPathDB; FungiDB:PADG_03472; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_1_0_1; -.
DR InParanoid; C1G5A2; -.
DR OMA; RHYTIDY; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000001628; 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; 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:UP000001628}.
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..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 1066 AA; 120115 MW; 9A98CE4AC1270FCC CRC64;
MAPGSEAVGA SSHDKRNGQM NGKPKTSSPP WAKRSNGRRI KRQEVERTFA KYAEFSGDFT
QVKKVVSNGI FKEVKWMGWK GIRTLLAVVK SKTSGKLTDD KEYLMERIIQ LVASLPPEST
ARVKLTNSFV KSLWVSLPHP PLSYLGDEYR YRAADGSNNN PLFPRLGAAN TAYARSIKPS
TIQPAALPDP GLVFDSLFAR QEFKPHPNGV SSMFFNWASL IIHDLFETDP RNQHISLTSS
YLDLSTLYGD NQQQQDDMRT FKDGKLKPDT FADPRLIALP PGCSVILILL NRFHNYVVEQ
LAHINENGRF TKPRDDLASE DSRNAWAKYD NDLFQTGRLI TCGLYINITL YDYVRTIINL
TRTNTNWSLD PRVNMKKGAK PEAAESGVGN QVSFEFNLAY RWHSTIGEID EKWIGEVYLD
LFGKTAEEIS MEELIAGMGK WKRNLPKDPA QRTFAKLERQ ADGRFKDEDL VRIITEATEE
VAGTFGPRNV PKALRAVEIL GIHQARKFGC GSLNEFRKFF GLKGHPDYVE LYPGIVSEEA
KIPMVPGAGI CPTYTISRAV LSDAVALVRG DRFYTTDYNA KNLTNWGYAE SHYDLSVNQG
CMFYKLMLRA LPNYIKPDSI YAHYPMTIPS VNREIFTKLG RESHFSWDRP ALIPPRIDLT
SYNGTKTILE NVRDFRFTFG DVASSLFGSQ SFNVSQSEIL DETFRQDSWS QNVKKFYEDI
TLNLLKQNSV RVAGINQIDI TRDVGNLAHV YFAASTFDLP LKTKENPKGL FTDREMFMVI
VAIFTSVFFD VDPTKSFALR QVTREAGEEL GKVVESYVKS AKGFISLSGI VDRFQKHDNP
LAKYGLDATR KLLKCGLSVS EVAWSQLLPI ICTAVPSQAQ VFTQIIDFYL SDEGKPHLPE
INRLAHEDSP ESDAKLLHYC MEGIRLNGTF KSYREANTNV LINDTGRDVV VNDGDKVFVN
MISSSRDPNI FPSPDDVVLD RPLESYIHFT DSAFTCFGRG AHMVALSSML RVVGRLDNLR
AAPGPQGRLV KVIRPNGHFA YMREDYGGYS VLPMSEFFTC FFAVKS
//
