ID A0A179U9R3_BLAGS Unreviewed; 1034 AA.
AC A0A179U9R3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=linoleate 8R-lipoxygenase {ECO:0000256|ARBA:ARBA00013239};
DE EC=1.13.11.60 {ECO:0000256|ARBA:ARBA00013239};
GN ORFNames=BDBG_01248 {ECO:0000313|EMBL:OAT04746.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT04746.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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}.
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DR EMBL; GG657449; OAT04746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A179U9R3; -.
DR VEuPathDB; FungiDB:BDBG_01248; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000002038; 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:SF13; LINOLEATE 10R-LIPOXYGENASE; 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; PS00086; CYTOCHROME_P450; 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:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000002038}.
FT BINDING 330
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 1034 AA; 116257 MW; F32BD9B5ED882FAD CRC64;
MKHPPKNMDL KRVGDVVKFV KDTVKGKPMN DRLLAMENII AIVGALPPNS KHRIKLTNIL
ITRLWDSLEH PPINFQGPKF YYRTPDGSYN NVHFPNLGKA GMPYARSIRS DTKLPGVRPD
PGLLFDLLMK REDGKFKQNE GGISSLLFHH AALIIHDIFR TDRRDMNINN NSSYLDLSPL
YGSSLKDQLK VRTMKNGFLK PDTFHDERLI AQSPGANVLL VLYSRFHNYV AETLLLINEG
GRFTPKGDDE ASLAQLDEDL FQTARLIVGG LYINISLHDY LRAITNTHHS DSSWTLDPRV
DIPASLVKSG PERGIGNQVT TEFNLLYRFH SCISLGDEKW LDEFFGEIFK STGKPLEELT
LKDGMRAIAQ FESLIPMDPS QRNFGGIERG EDGRFRDEDL VRLLKASIDD PAGAFGPKNT
PKAMRVVEIL GIHQARQWRT ASLNEFRKFF KLKPHETFED INPDPEIADH LRNLYGHPDM
VEAYPGLYVE DAKPRMDPGS GVCTPYTVGR AVLSDAITLV RSDRFNTTEY NVATLTNWGM
AEAQQDYDTL GGSMFYKLIQ RGLPGWFPFN SLSVMQPMYT PAMNREIATE LGTISQYTEA
DPKPPPRRLV LMKHSEISQM LSDPKQFPVP FGKPYENFIE GRDFGHFMLA GDMPRNKEQR
NLYGSALYGS GELKELLSTF IVDQTDKFLT GSMFQIGRGT YHVDILKDVA IPVMTRFMGD
LFQFDLKTEE NSSGTYDIDG LYNDLLNIRI WGFGNDDPAL SWNRRRDAQA SARRLLASTE
AYIKRVTSST RIRNIVGAVT NGLASNGNST SLRSFGRDCI MELLSNGKSV QEIADIMVFT
ALGGIGAAIS TLAEVLEFMI AVPENVEHLE AFQQLTLENS ERADNDLRRY VLEMQRLTAG
HVTIRVATQP GGFGAQSFQP GEQIIAYFAA ACRDPEAYPE PEKIKLDRPL EKYIAFGDGP
HQCFGRELAL AFLVGVLKRV TALKNIRPAL GGMGVLKKIK RNGIPYYLSE DWSSFTGYAS
TWQLQFDDPD FVVS
//
