ID A0A0D2A2K4_9EURO Unreviewed; 1155 AA.
AC A0A0D2A2K4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Linoleate 8R-lipoxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV07_01282 {ECO:0000313|EMBL:KIW34506.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW34506.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW34506.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW34506.1,
RC ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; KN847040; KIW34506.1; -; Genomic_DNA.
DR RefSeq; XP_016254722.1; XM_016387794.1.
DR AlphaFoldDB; A0A0D2A2K4; -.
DR STRING; 569365.A0A0D2A2K4; -.
DR GeneID; 27340476; -.
DR VEuPathDB; FungiDB:PV07_01282; -.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000054466; 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:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 405
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 1155 AA; 128504 MW; 91BA0AD345E7B313 CRC64;
MARKRKLSST SLDAMDGSRD LPSGSGDDNT GYRISTTIRS FFESIAGSSS ESTSTVINGA
TVQSRPLLAR VLADVASQAP RIGENLGLLG SLVDTTLFDG GLVDDRQYQM EKILQLAASL
PPGSKSLDDL TNQFIKLLWE NLEHPPLSYQ GDDYKYRTAD GSNNNIMYPH LGKAGSYYAR
TVTPQTLKPG VLPDPGVIFD AIFARGEEPR EHPNKISSML FYLATIIIHD CFHTDETDYS
TVKTSSYLDL APLYGSSQEE QNQIRTFKDG LLKPDSFCEK RILGFPPGVS AIIVCFNRFH
NYVAMQLKEI NEGGRFKLPK NDQDTAAIAK LDNDLFQTAR LVTCGLYVNM ILNDYVRTIL
NLNRTNSTWT LDPRKNFSDV FDSAGIPSGV GNQVSVEFNL VYRWHSAISI KDEKWTNELY
QSLFPGRDVS TVTEWELLPK LKKWLDDRGP DPAKWDLDSG RYKRTQRGTF RDEDLIKILT
EATEDVACAF GPRNVPLVMK LIDVLGIQQA RAWNVATLNE FRKFFKLEPH TTFSDITKNT
EVARSLKALY GHPDYVELYP GIVAEDAKDP LEPGSGLCPG YTISRTILAD AVALTRGDRF
YTVDYTPANL TNWGWSQVKS DPTVAQGGCF YTLLMRALPF YYRGNSVYAM FPLTVPEENR
KILTKLGKDQ DYNFDRPSYV GVPTSIRSWK AVTGVLGDQA SFGVPWGPHT FYLTHQDYML
SGDSVANATQ RKEVQNALYC PVNGLAQVQK FYEDLTTQLV VARSERLRGE WYQLDACRDV
GNPSHAIFVA RLFHLPLKKP GDLNPIGVEV DQLYLALSIE FAYVFLDLDT ASSFKLRAGA
KTANDQLSKL VKIVCEAVKV GGILRVRDLF SMGTTGELLS DYGTLLLKRL FEGGKSVEEV
VSTIIPTAAA AVATQAQHFT QMLDVYLSDE YKEHWPEIQR CAWSNNPADF EKLKGYALEA
NRLAPAAFGL LRKANIDTVI PDNGQKVPVK AGDQIYVDFI AAGLDESVFP NPHTIDPTRD
RSLYIHHGYG PHACLGRPMV EVAMAAQLKV FAKLKNLRRA PGPQGQLKKT VPAPNPTSSD
PKANPGTVEV FMLEDWSSWY PFPTTMKVHH DGLWKDQPDE LAGETGVPGI QEQIMNSDMA
AANGLNGDYM EEDTA
//
