ID A0A1Q8RWM4_9PEZI Unreviewed; 1172 AA.
AC A0A1Q8RWM4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=linoleate 8R-lipoxygenase {ECO:0000256|ARBA:ARBA00013239};
DE EC=1.13.11.60 {ECO:0000256|ARBA:ARBA00013239};
GN ORFNames=CCHL11_06004 {ECO:0000313|EMBL:OLN89044.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN89044.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN89044.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN89044.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLN89044.1}.
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DR EMBL; MPGH01000084; OLN89044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8RWM4; -.
DR STRING; 708187.A0A1Q8RWM4; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000186583; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR002048; EF_hand_dom.
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; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS50222; EF_HAND_2; 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:ARBA00022964};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000186583}.
FT DOMAIN 472..507
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 426
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 1172 AA; 131701 MW; FD3D1C81E5D2632F CRC64;
MSQAEEQFPK TQPPLTERLA AARKVLQKSI SPIPQHAGPV PGGASEEAEP TNLLQDIKKL
GFEDFDTLGN FLGSAVRGQI NDNELLLEHL IQLFAKLPAG TVKGKKLESG LINQLWNGID
HPPMTTLAEE HKYRAADGSN NNIHAPRMGA AGTAYARSAP PVAYQSPNQP EPSLIFDMLF
ARGPEFKPHP NKISSVMFYL ATIITHDIFQ TDGLSGINQT SSYLDLAPLY GRNQKEQDAI
RTKRDGRLKP DSFSSKRVLG FPPGVGVLLI MFNRFHNYIV TNLASINENN RFPKPTTDPI
DVSKPAPEKP VAPKKPENVG DDSPEYQEYL SLQKEYDALK KDYDSWNAWV KYDNDLFQTG
RLITCGLYVS IVLRDYVRTI LNLNRSSSSW ALDPRTNEGK SILTTETPEG TGNQVSVEFN
LIYRWHCTIS PKDDKWTQDV FSKVLKHPTG KPVSEFTLRE FGEAVRGWER EIPDDPIKRG
FSDLDRNTDG TFREEDLVKI FKESVEDVAG SYGANRIPEI MKPIELLGIQ SARNWNVATL
NEFREHFGLT RHPTFEDINP DPEVAAKLRF LYGSPDLVEL YPGLVAEKAK PPMAPGSGLC
GNFTMTRAIL SDAVALVRGD RFYTVDYTPK NLTNWGFNQA SYDHNVDQSH VFYKLVFRAF
PNSFQQNSIY AHFPFTVPSE NKKILDSIDR SYLYSWEEPK LRTPMIPILS HKAVSDILYN
QTDFKVIWGD AIRHLVAQPG KDYSKNFCLS GDGKANAMNR TVVRKALISG PWEQEVFKWY
THMTPRLIKQ HSFPYVKGKR EVDVVRDVIN LTNTRFNAAL FCLPIKNEDS PWGVYTDQEL
YMVVATLFQC VFLDADIANS FKLRTIAREL GQDIGKLMTL VVQTISKAGL ITDIVAKIRE
GEASLPTFGN HLIERMLADG QDLDEVVWGT IMPVVTANVT NQSQVLSLCL DYYLGDGSKH
LKELYRLAHE NTPETDELLM KYMLEGCRLR GPVAVYREAA TNQVITDYAP ALPNPNDPTS
RNPVVNPDID GSKYEVKISK GQRVICNLMT AGRDPSIFED PNEVRLDRPL ESYVHFGLGP
HWCAGKEISR VAQTSLFKQI VGLKNLRRSE GGRGQLKNMP AGAWGGQVGL PVEGQNGASS
RQQPWLGLRA FMTADQSSYW PVPTTMRVQW DE
//
