ID A6QWB2_AJECN Unreviewed; 1030 AA.
AC A6QWB2;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=linoleate 8R-lipoxygenase {ECO:0000256|ARBA:ARBA00013239};
DE EC=1.13.11.60 {ECO:0000256|ARBA:ARBA00013239};
GN ORFNames=HCAG_01669 {ECO:0000313|EMBL:EDN03804.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN03804.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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 -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; CH476655; EDN03804.1; -; Genomic_DNA.
DR AlphaFoldDB; A6QWB2; -.
DR STRING; 339724.A6QWB2; -.
DR VEuPathDB; FungiDB:HCAG_01669; -.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OMA; KIQWDGD; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000009297; 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: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; 2.
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; PROSTAGLANDIN G/H SYNTHASE; 1.
DR PANTHER; PTHR11903:SF37; PSI-PRODUCING OXYGENASE A; 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; PS00086; CYTOCHROME_P450; 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:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1030
FT /note="linoleate 8R-lipoxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002698845"
FT BINDING 361
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 1030 AA; 115254 MW; 73D9F5B29088A843 CRC64;
MTIGLKKWAV SLCARALLLP IVAAVKITSR MTGSCGKKAL REEIEDGVLK LSQLIHSLLR
PLPTQTGDGT YVDETPPEPS LIDDLNQVDI KDLETLADVI RNAATGAPVN DKDYIMERII
RLPSSLPSRS PNVDRLSNAL LSLLWNDLKH PPLSYLGEQT SFGHKLALQV LHMQGLYHRS
RSNQQCSQIR GSFSIIYSAL TAMIIHLAPL YGSNQEEQNT VRTFKGGKLK PDCFSEKRIL
GFPPGVGVLL IMFNRFHNYV VENLALINQD NRFPKPAEPS GKAYAKYDND LFQTGRLITC
GLYINIILKD YLRTILNINR TDSDWSLDPR SESMRGLFGT AIDEAGGNQV SAEFNLVYRW
HSCVSERDDK WTQNAYRELF GDGMDPNKIS LSDFLRVLGK WEAGLSKDPL KRPFAKLARG
SNGLFNDDDL ANILTESIED CAGPFGTSQI PAVFRAVEIL GINQARHGDF RASTNNVELY
PGPIAEEAKE SLVPGSGLCA NFTISRAILS DAVALVRGDR FYTVDQTPKN LTNWGFNEAS
YDNTVDKGHV FYKLFLRAFP SHFKPNSIYA HFPLVVPDEN REILTRLNSS RKYSWDKPAR
IPRPTMIESY AACDAIIKNQ KDFKVTWGEA IEFLMHKECH SFGRDFMLSG DEPPNAASRQ
MMGRALYHGE WEAEVKKFYE QITLKLLHAK SYKIAGVNQV DIVRDVANIA QVHFAVAVFG
LPLKTGDNPR GIYTESELYM IMALVFACIF FDADPAKSFP LRQRARKVTQ QLGDIVLLNV
QLIKQTGFLS NMVERLYGNN MLTEYGVHMI RRLLDSGLPP EQIVWTHMLP TAGGMVANQA
QLFSQCLDYY LSEEGSIHLP EIHRLSKLGT AEADELLLKY FLEGSRLRAT VGVYREVVTQ
STIKDGVKTL SLKPGDRVAC NFAKASMDPK KFPEPDKVDL TRDLDSYIHF GQGPHKCLGF
GICNAALSTM LKTVGKLENL RRAPGPQGEL RRIPGPGGIS KYLVVDYTSY FPFPTTMKVQ
WDGELPPCAN
//