ID V9DCW7_9EURO Unreviewed; 1063 AA.
AC V9DCW7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Linoleate diol synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=G647_03890 {ECO:0000313|EMBL:ETI24521.1};
OS Cladophialophora carrionii CBS 160.54.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1279043 {ECO:0000313|EMBL:ETI24521.1, ECO:0000313|Proteomes:UP000030678};
RN [1] {ECO:0000313|EMBL:ETI24521.1, ECO:0000313|Proteomes:UP000030678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 160.54 {ECO:0000313|EMBL:ETI24521.1,
RC ECO:0000313|Proteomes:UP000030678};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora carrionii CBS 160.54.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; KB822704; ETI24521.1; -; Genomic_DNA.
DR RefSeq; XP_008726457.1; XM_008728235.1.
DR AlphaFoldDB; V9DCW7; -.
DR GeneID; 19982383; -.
DR VEuPathDB; FungiDB:G647_03890; -.
DR HOGENOM; CLU_002329_0_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000030678; 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; 1.
DR Pfam; PF00067; p450; 1.
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}.
FT REGION 9..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 366
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; 118688 MW; F3DF636C01C17D02 CRC64;
MEKLHKLQAT IFQQAPTAPD GRTDAEAAAT PPVTQTSLLH DLTHLGRENA ATMVQAFTTL
ISGEPLNDKE LLLEHGVHML QSLPPNSGLG AKAAGGFIKM LWDDLPHPPG TIAGPTTRYR
RHDGGSNNLW DSELGKAGSP YSRSVPPMKP KGPNLPDVEL VFEYLLKRKE GKFRKHPSGL
NRLFFSFATV VIHECFQTSR DNKWVNETSS YVDLSTLYGN TAKEQERVRT YKNGLVYPDS
VASERIMLMP PGVIAVLMMF SRNHNHIAET LLSINEQGTY GEWDRLTEDK QKKQDEDIFQ
LARNINVGFF ALVVLRDYVA AILNTPRANS DWSLNLGEEI KSAQGRVERG SGNAVSVEFA
VLYHWHAALS AADAKWMEDM ISQYGPRLNS LDEMTPKDFW EMAANITKEM MSKPAKEWIF
GGLKRGPDGR FDDADLGRLI KDCIEEPAHA FGANGTPASL KVVDLMGQLQ AREIFNVCTL
NEFRKYLNLT AYKSFSEWND DPEVSRAAEL LYGHIDNLEL YPGLQAECTK PPMPGSGVCP
GQTTGRGILD DAVALVRGDR FLTYDFNSNT LTNWGVSKLA DLPGGTYGGI LAKLIFNGLP
GEFTGTSTYA LMPFYTPEAI KGILEGNKAL AKYDLKRPPP NVMKLVGIHT QEGVKKAFED
RDTFHVMYQA AIRNCTDGHE FMIGWDDRKR HDPRSDTLHK VFFEDNFEKN LSQYFRETVR
SLIQKSTLKY HDERRSIDIV RDVCNVTPIM WLARRFAIPI KDVAHPRGLV TIPELFDIFL
VLFMYQSFNI LPVNEWKLRE AAGTVAPILR KIFETHLKTQ QGFTEHIVDW LTKGSAYEVG
PDADRFYHAL NKTGMNIGDM VGDCIGMGAP VAGNITQQAS LLIDLYLKDE YKQYKARIVE
LAHKDDEASD KELLGFVFEG MRHAGVVPGL PRVASKDVTF EDGARGPVHI KGGQYVLIAT
SSAAMDPAAF PDPEKIDPHR PMSSYTLLGH GMHYCFGARI VGPALVATLK EVFRLKNVRR
ANGRLGHFSV IEHDIAGVKA KIYLDANAKE SPIPTTLHLL YDE
//
