ID N4WHL7_COCH4 Unreviewed; 1184 AA.
AC N4WHL7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=linoleate 8R-lipoxygenase {ECO:0000256|ARBA:ARBA00013239};
DE EC=1.13.11.60 {ECO:0000256|ARBA:ARBA00013239};
GN ORFNames=COCC4DRAFT_45848 {ECO:0000313|EMBL:ENH98714.1};
OS Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665024 {ECO:0000313|EMBL:ENH98714.1, ECO:0000313|Proteomes:UP000012338};
RN [1] {ECO:0000313|EMBL:ENH98714.1, ECO:0000313|Proteomes:UP000012338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 / ATCC 48331 / race T {ECO:0000313|Proteomes:UP000012338};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000012338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 / ATCC 48331 / race T {ECO:0000313|Proteomes:UP000012338};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (8R,9Z,12Z)-8-
CC hydroperoxyoctadeca-9,12-dienoate; Xref=Rhea:RHEA:25395,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:58659;
CC EC=1.13.11.60; Evidence={ECO:0000256|ARBA:ARBA00000699};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; KB733505; ENH98714.1; -; Genomic_DNA.
DR RefSeq; XP_014072624.1; XM_014217149.1.
DR AlphaFoldDB; N4WHL7; -.
DR GeneID; 25845233; -.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000012338; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0052878; F:linoleate 8R-lipoxygenase activity; IEA:UniProtKB-EC.
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:UniProtKB-KW.
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; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS00018; EF_HAND_1; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022559};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559}.
FT BINDING 443
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 1184 AA; 132248 MW; 50A0E96D8E03F6EB CRC64;
MVVNNLELGV AALASAATVV LYNYSGDIAK ATAPDHKYQA GEDYHSEKKK AKNFFADPKA
ITAALLRDYA SVRSKIKPHE LLPIVQDLLK KGEPIDDKAG STEKLIHVLT TLPEGSQTRI
NLTNKLIDTL WDNLQHPPLS YMGGSLKVKI EGDKTEVRLT DTITYKSPEN GVEITETMPL
RPHAMHQYRT PDGSYNNILS PDLGRAGTPY AKSVLTSKKL HGVKPDPGLL FDLLMAREEG
TFKENPAGIS SILFYHASII IHDIFRTNRT NMNISDTSSY LDLAPLYGSS LADQLEIRTM
KEGKLKPDTF HEKRLLGQPP GVNVMLIMYN RFHNYVAEIL LKINENGRFT LAKFENPSPE
DIARAVAKQD HDLFNTARLI VGGLYINICL HDYLRAITNT HHSDSNWTLD PRVDIDKHFD
PNGAPRGIGN QVSVEFNLLY RFHSCISKRD EKWTEDFFQS EFPGKTIDEI NKLDLYELLG
GLQKFFGNVN PDPSKREFGG LRRQENGMFN DEELVRVMKE GMEDPAGCFG ARNVPKALRV
VEILGIVQGR KWQVASLNEF REFFGLKRHA TFSDINSDKD IASVLEKLYT HPDMVEMYPG
IMIENHKPAM DPGCGICPTY SVGRAVLSDA ITLVRSDRFN TLDYTVSNLT AWGYNEVQQD
YKTLGGSLFY KLIQRALPGW FPFNSLHVMQ PMYTKKANEA IAKEIGTISL YTEADPKPPR
PVHVLAEGIS VREVLHDERF VVPWLPAVND LFPGSGKDFS WFMLAGDKPE NAAQKRMVQE
VFHSIPGFEA AISSFVAEVG SKLLAKETFK MKEGLNQIDI IRDIAIPMNA QLLSDIFYLD
LRTDENKSGS LSTAEFYKHL LNIRIWGVNN NDPAMAWNRR RWAQEGAAIM TKSGRDLVRD
VANEKGASGF AGYLASAISD KHKSRSSEIK QNSLRSCGHK IVQGFLSKSI SPEKTADICW
LTAFGGIGVP VTTLCEIMQF FLNENNKKHW SQVQSIAAAG DDQTLRLYTL EAMRLTTAQR
NLRIATQPAM IDGKDIKPGD AVLLLLGQAG RDPSVVQDAD KFIPTRKQDG LITPFSTGPH
DCVGRQIAMN FIVGMVKLFA GLKDLRPAPG QMGIVKTIQV GTERCYLNDS WSWLSFDAST
WKLHFSGHGK GSFKAPPAHI GENLELSQIE AILGKNKDEK NLID
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