ID A0A0D2CPX8_9EURO Unreviewed; 1165 AA.
AC A0A0D2CPX8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Linoleate 8R-lipoxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV05_10662 {ECO:0000313|EMBL:KIW51997.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW51997.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW51997.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW51997.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; KN847322; KIW51997.1; -; Genomic_DNA.
DR RefSeq; XP_013312582.1; XM_013457128.1.
DR AlphaFoldDB; A0A0D2CPX8; -.
DR STRING; 348802.A0A0D2CPX8; -.
DR GeneID; 25332570; -.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000054342; 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: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:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 462
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 1165 AA; 131374 MW; 0EBB8AB5A11F487D CRC64;
MPLLRRLSSS FKKKMVTQKN RATANGNLTP VDEAGAPEQN GTQPGCSVAQ SLAKTKDVHW
NTSYNPPSPS AAQEPVTAGA GAGASGPATR KDVENFFQEF AQLLHASRRT LPTQSGDGQY
LDQAESSGLL ADLKSLGLKD VKTVTHMLED KASGKAQDDR ELHMEEIMQL IAALPDRSAN
RVELTSMLLD VLWNSLQHPP MSYLGDTFRY RSADGSNNSY IFPKLGAANT PYARSVSPVI
VQPGALPDPG LIFDSLLARE DFKPHPNKVS SIFFNWASLI IHDLFQTDHH DYSISKTSSY
LDLSILYGDT QSDQNNMRTF KDGKIKPDCF AEERLLAFPP ACGVMLIMLN RFHNYVVEQL
ALINENGRFT RPSDRLPKDG APAAWRKYDN DLFQTGRLIT CGLYINITLY DYLRTIVNLN
RTNSTWTLDP RLDKPKTFGS DGTPRGIGNQ VSAEFSLSYR WHSCIGQMDE AWTEMVYQEL
FGKAPDSVSL QELMAGLGKY DHELPADPLA RPFAHLKRCA DGKFDDGDLS KIMQAGVEEV
AGAFGARNIP KCLRAITILG IMQGRSWNLC TLNEYRKFFG LKTYDTFEEV NRDPHIAEQL
KHLYEHPDYI ELYPGLAVEE YKEPMAPGVG ICPTHTVSRV VLSDAVALVR GDRFYTLDYN
PKNLTNWGYL EVAYDLGVNQ GCVFYKLILR TLPNHFMPNS IYAHYPMTVP AENAKIMQNL
GRYHDYDWSR PTYIPTRVNL TSYQSAKYLL ERSQDFTVMW NDGLSFVMGE GGRKFCLGGD
TVLHRKQREL MHGLLYREKW HEHIKNFYEY ITLRLLHEKS CTIAGINQVD LTRDVGNLAH
VHFAANVFSL PLKTAENPAG IFTEQEMWMA MSVIFTAIFF DFEPTKSFPL RLVARKLATM
LGKLIEINVK SVTTTSFASN FLDSFRENEN ALAEYGIHMI RRLSQSGMST YDVGLSQIMP
TAVAMVPNQS QVFSQIMDHY LSDEGLEHLP EIQRLARIDS RESDEKLLRY VNEGIRLNGT
FGSYRRSEVS HVFNDDGRQV AVKPGDKVFC SFVGAARDPN IFPNPDRVRL DRPRDSYLHY
GIGDHTCLGK EASMVALTAM LRTVGKLQNL RRAPGPQGQL KKVPRPGGFY VYMRDDHGSY
FVFPCTFKVH YDGPLPSFRR GRAEH
//
