ID A0A0D2IU20_9EURO Unreviewed; 1167 AA.
AC A0A0D2IU20;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Linoleate 8R-lipoxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z518_00639 {ECO:0000313|EMBL:KIX09559.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX09559.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX09559.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX09559.1,
RC ECO:0000313|Proteomes:UP000053617};
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 Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; KN847475; KIX09559.1; -; Genomic_DNA.
DR RefSeq; XP_013276695.1; XM_013421241.1.
DR AlphaFoldDB; A0A0D2IU20; -.
DR STRING; 1442369.A0A0D2IU20; -.
DR GeneID; 25288710; -.
DR VEuPathDB; FungiDB:Z518_00639; -.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000053617; 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:UP000053617}.
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 464
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 1167 AA; 132497 MW; FCBCB49522179C50 CRC64;
MALLRRLSSR FKSTSDNRNS INGTNGPLPL ANEPKGPPAA NDHQINGSHA NSAIVGPNVE
KTKNVRRLSF RPTVSSPPPG QPAEDHGPPA TRKDVESAFT QFAQLIHASQ RPLPTQSGNG
SYLEKEEPSG LWADLRSLGL KDIKTVRHML EDKASGEPQD DRKMHMEEIM QLLAALPDRS
ANRVELTSML LDTLWNSLQH PPMSYLGDDF KYRSADGSNN SYIFPKLGAA NTPYARSVNP
VTVQPGALPD PGLLFDSLMA REEFKPHPNR VSSIFFNWAS LIIHDLFQTD HKDYTNSKTS
SYLDLSILYG DTQEDQNTMR TFRGGRIKPD CFAEERLLAF PPSCGVMLIM LNRFHNYVVE
QLALINEGGR FNKPSDHLPE EAKKAAWKKY DNDLFQTGRL ITCGLYINIT LYDYLRTIVN
LNRTNSTWTL DPRLDKPKTF GNDGTPRGVG NQVSAEFSLS YRWHSCIGQM DEAWTEAVYR
ELFGKSPDDV SLRELMIGLG KYDHDLPADP LQRPFAHLKR DAHGKFDDGD LARIMQDGIE
QVSGAFGARN TPKSLRAITI LGIMQSRSWN LCTLNEYRKF FGLKTYDTFE EVNRDPYVAE
QLKHLYEHPD YIELYPGLAI EEYKEPMVPG VGICPTHTIS RVVLSDAVAL VRGDRFYTLD
YSPKNLTNWG YNEVAYDLSI NQGCVFYKLI LRALPNHFKP NSIYAHYPMT IPSENAKIMK
NLGRYHDYDW ETPSYIPTRI NLTSYQSAKY LLERPQDFTV MWNDGLGFVM GQGGEKFCLG
GDTVFHRKQR QTMHQLIYRD KWHEHVKHFY EYTTLRLLHE KSRKIAGINQ VDLTRDVGNL
AHVHFAANMF ALPLKTAENP KGIFTEHEMW MAMSVIFTAI FFDFEPTKSF PLRTVAKKLA
TMLGKLIEVN VKSVTATSFA SKFFDSFREN ENALADYGIH MIRRLSETGM RAYDMAFSQI
MPTAVAMVPN QSQVFTQIMD YYLGVEGIKH LPEIQRLARI DSEESDDKLL RYVNEGIRLN
GTFGSYRRSE TDHVFNDDGK QVPVKPGDKV FCSFVGAARD PSVFPSPHEV RLDRPLDSYI
HYGIGEHTCL GKEASMVALT AMLRTVGKLE NLRRAPGPQG QLKKVPRPGG FYVYMREDHG
SYFVFPCTFK IHYDGTLPPL PKPKAEH
//
