ID A0A0G2HKH9_9PEZI Unreviewed; 1115 AA.
AC A0A0G2HKH9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=linoleate 8R-lipoxygenase {ECO:0000256|ARBA:ARBA00013239};
DE EC=1.13.11.60 {ECO:0000256|ARBA:ARBA00013239};
GN ORFNames=UCDDA912_g04499 {ECO:0000313|EMBL:KKY35538.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY35538.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY35538.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY35538.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY35538.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY35538.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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:KKY35538.1}.
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DR EMBL; LCUC01000155; KKY35538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2HKH9; -.
DR STRING; 1214573.A0A0G2HKH9; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000034680; Unassembled WGS sequence.
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; 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 SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022559};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680}.
FT REGION 19..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1115 AA; 123947 MW; CFABFC6326212320 CRC64;
MSTSADGRLS SIVETVRASL APPNKSSSQA SANDDDTSQT GLISDIRSLG FEDYGTLMQF
LNTSVTGIND DNNHLLERLV QLLAKLPPHS KQMKGLSGGF INQLWATLDH PPVSSLGNQY
KYRRADGSYN NIHAPHVGAA NTPYARSVRP TVFQNPDLPE PEIVFETLMA RGDKFTPHPQ
GISSMLFYLA TIIIHDIFQT SHADYSINLA SSYLDLSPLY GRNEYEVNMM RTFQDGLLKP
DCFSSTRILG FPPGCGVFLV MFNRFHNYVA TQLALINEVG RFDKPKAGDK EAWAKYDEDL
FQTSRLVTCG LYINIIMKDY EGRDMFSKPV PEGVGNHVSA EFNLVYRWHS TISLRDEQWT
IAEMRRLLKG KDPVTASVED VLRALGEWQA DLPARPEART FENLTRLPDG TLSDDDMVKI
LTEAIEDVAG SYGANRVPRC MKSIEILGIL QARHWNLGTL NEFREFVGLT KHGSFEDINP
DPDIVAHLRR LYDSPDCVEM YPGIVAEKTK PPMSPGSGLC GNATMTTAIL SDAVALVRGD
RFYTVDYTPK SLTNWGFNEV NYDTAINGGH VMHKLIFRAF PNNFANNSIY AHFPLVTPSE
NKKILEGLGT RSQYSWEAPR ARPFPVMIKS HKACTQILND NTSFKVAWGE AITSLTHNHD
APGLSAGFCL SGDRNANRSN RDYIQKCLYP DRWDSDVKAF FSTTSSRLLS RYGYIAPDKP
EGRTREVDIV RDVIALATTH FSAAVWSLPI KTEANTHGIY TERQLYSVLL AGFAAIFFDA
DIANSHKLRS QSRVLAQQLG RLMTLKAKLL GAGDGIVAAM LDTVKESITT IGHIVNRNET
RKASSSSEHE WPVLALYGDR MIKRMLSENG ATPEQVIWGS VLPASVAACA NQTQVLSQAI
DYYLGEGMEH LPAMYVLAHQ DTEDSDEKLK KYMLEGVRIR GEVAITREVV KDQAVRDFSP
SQPDPSDPRG LNPLPNANPG GSGTTHELRA GARLLLNLTA ANHDGTVFPE PETVRLDRPI
KSYIHFGWGP HLCLGQDMSI VGLTVVFKKI VGLKNLRRAP GGRGEIKSFP VVFWNGQVRG
KRNPDAGWTG LRTYMTADQS SFWPIPSTLR VQWDE
//
