ID A0A0C9XJ66_9AGAR Unreviewed; 1063 AA.
AC A0A0C9XJ66;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Linoleate 8R-lipoxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=K443DRAFT_678358 {ECO:0000313|EMBL:KIK01489.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK01489.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK01489.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK01489.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; KN838606; KIK01489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9XJ66; -.
DR STRING; 1095629.A0A0C9XJ66; -.
DR HOGENOM; CLU_002329_0_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000054477; 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 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:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000054477}.
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 382
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 1063 AA; 118348 MW; 0669377DA83D48CF CRC64;
MSVNRLSSFL GRRPSASTNG VVNGSVTATS PTKDAPGDTP KVLKDFREQI KRGVPFSLET
SSLAAILDLI RHKDAIDDRK LLLEHALTFV SRLEESDFSL KLRNGIIELL YNDLTHPAAT
SISNKYAWRT ADGSFNNIDV PDMGKAGTPY SRSVQQANPL PKNQLPDPGL VFDTLLKREG
FVKHPGGLSA LMFAFAALVI HSVFRTSHRD VNINETSSYV DLAPLYGNNL EDQNRVRKRD
GRGRLHPDVF AEDRLLLLPP QVCSLLVLFS RNHNYIVERL FEINERGTYV DPDQLSPDIP
ASKAKLLAQE EDLFQTARLI NCGWFGSIVF SDYFSCILGL VRDGNNWSLS PFGEIRKDDH
SLFERGKGNV CSVEFNCLYR WHATTSLEDE AWVHTAFSQI FGGKPIDQIT PDDFRNAAGK
MERDLPENSK WTFGGLQRQG NGQFKDADLA DVLKNATEHS AGAFRARGTP AAMRLNEVMG
IEQNRRWGVC SLNDFRKYLG LKPYATFLEW NSDPEIADAA ERLYGNINFL ELYVGLQAEE
AKPLVEGAGL CPGYTVSRAI LSDAIALTRG DRYFTHDFTP FNLTAWGFAD CQRDPNAFGF
GSTLGRLLLR TLPNDYTENS VYTFFPLMTP ESMKTNLTKL NLLDKYDLSR PQTRTPLRIV
SDHSEVVKLL NDKESTSKPY AARVARVIKG KGFFPAEGGK EQEAVTTALS GSQELVDDIG
KYFYETTKKL IVGHSFTLVG GKVAGVDLVK HVLRVVPVLW VATDLAGIEL KTKSHPHGPY
TPSELFDVLG EIYSFVFLDV ELAQVMVLQE NIKSHVKKLL RLIKGGLDGG AGNRLSIAGI
VETVSSLFSK PKKSDHSVLM KRLHELGQSH DQLANTVLAL MVGASVELSL SLTNMVNLYL
GSDKHEQITA LAKNPESSLR GYVYEALRID PPFEGVYRIS TKDQTIAGQT VNKNDRIFVD
IGTANLNEKV FPHPVSVDIS RSTKEALFAE GVFEYLGEHL TVKVMSEVLR AVFDLNNVSR
APGQSGVLKR FKVHTRPECR YGYLNHSQIA YEWPTSMSIQ YSK
//
