ID LIDS_GAEGR Reviewed; 1165 AA.
AC Q9UUS2;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Linoleate diol synthase {ECO:0000303|PubMed:8662736};
DE Short=LDS {ECO:0000305};
DE AltName: Full=Linoleate (8R)-dioxygenase {ECO:0000303|PubMed:8662736};
DE Short=Linoleate 8-dioxygenase {ECO:0000303|PubMed:8662736};
DE Includes:
DE RecName: Full=Linoleate 8R-lipoxygenase {ECO:0000303|PubMed:8662736};
DE EC=1.13.11.60 {ECO:0000269|PubMed:8662736};
DE Includes:
DE RecName: Full=9,12-octadecadienoate 8-hydroperoxide 8R-isomerase {ECO:0000303|PubMed:8662736};
DE EC=5.4.4.6 {ECO:0000269|PubMed:8662736};
OS Gaeumannomyces graminis (Turf grass take-all root rot fungus)
OS (Rhaphidophora graminis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Gaeumannomyces.
OX NCBI_TaxID=29850;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=CBS 903.73 / DAR 23471;
RX PubMed=10497176; DOI=10.1074/jbc.274.40.28219;
RA Hoernsten L., Su C., Osbourn A.E., Garosi P., Hellman U., Wernstedt C.,
RA Oliw E.H.;
RT "Cloning of linoleate diol synthase reveals homology with prostaglandin H
RT synthases.";
RL J. Biol. Chem. 274:28219-28224(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=8662736; DOI=10.1074/jbc.271.24.14112;
RA Su C., Oliw E.H.;
RT "Purification and characterization of linoleate 8-dioxygenase from the
RT fungus Gaeumannomyces graminis as a novel hemoprotein.";
RL J. Biol. Chem. 271:14112-14118(1996).
CC -!- FUNCTION: 7,8-linoleate diol synthase is a bifunctional enzyme that
CC converts linoleic acid (18:2n-6) into 8-hydroperoxy-8(E),12(Z)-
CC octadecadienoic acid (8-HPODE) and then catalyzes the isomerization of
CC the resulting hydroperoxide to 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic
CC acid (7,8-DiHODE). {ECO:0000269|PubMed:8662736}.
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:0000269|PubMed:8662736};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate =
CC (7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate;
CC Xref=Rhea:RHEA:25399, ChEBI:CHEBI:57468, ChEBI:CHEBI:58659;
CC EC=5.4.4.6; Evidence={ECO:0000269|PubMed:8662736};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:8662736};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for oxygen {ECO:0000269|PubMed:8662736};
CC KM=8 uM for linoleic acid {ECO:0000269|PubMed:8662736};
CC Vmax=2.2 umol/min/mg enzyme toward oxygen
CC {ECO:0000269|PubMed:8662736};
CC Vmax=4 umol/min/mg enzyme toward linoleic acid
CC {ECO:0000269|PubMed:8662736};
CC pH dependence:
CC Optimum pH is 7.2-7.4. {ECO:0000269|PubMed:8662736};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8662736}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00298}.
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DR EMBL; AF124979; AAD49559.3; -; Genomic_DNA.
DR AlphaFoldDB; Q9UUS2; -.
DR SMR; Q9UUS2; -.
DR PeroxiBase; 4150; GgrLDS.
DR KEGG; ag:AAD49559; -.
DR BRENDA; 1.13.11.60; 2376.
DR BRENDA; 5.4.4.6; 2376.
DR SABIO-RK; Q9UUS2; -.
DR GO; GO:0052879; F:9,12-octadecadienoate 8-hydroperoxide 8S-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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; 1.
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; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Direct protein sequencing; Heme; Iron; Isomerase;
KW Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..1165
FT /note="Linoleate diol synthase"
FT /id="PRO_0000055599"
FT REGION 104..448
FT /note="Fatty acid alpha-dioxygenase"
FT /evidence="ECO:0000250|UniProtKB:G4N4J5"
FT REGION 666..1161
FT /note="Epoxy alcohol synthase"
FT /evidence="ECO:0000250|UniProtKB:G4N4J5"
FT REGION 1114..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 376
FT /evidence="ECO:0000255"
FT BINDING 203
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:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 379
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:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 1080
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 1165 AA; 128322 MW; 03D0B4170F56E452 CRC64;
MTVSTHHDDS PGLSGRLRDL LHHVFGNQKS PTVYPNAPGN SAKPVPTGLA DDIDKLGFKD
IDTLLIFLNS AVKGVNDDQQ FLLEKMIQLL AKLPPASREG KKLTDGLIND LWDSLDHPPV
ASLGKGFSFR EPDGSNNNIH LPSLGAANTP YARSTKPLVF QNPNPPDPAT IFDTLMVRDP
AKFRPHPNKI SSMLFYLATI ITHDIFQTSP RDFNINLTSS YLDLSPLYGR NHDEQMAVRT
GKDGLLKPDT FSSKRVIGFP PGVGAFLIMF NRFHNYVVTQ LAKINEGGRF KRPTTPDDTA
GWETYDNSLF QTGRLITCGL YINIVLGDYV RTILNLNRAN TTWNLDPRTK EGKSLLSKPT
PEAVGNQVSV EFNLIYRWHC TISERDDKWT TNAMREALGG QDPATAKMED VMRALGMFEK
NIPDEPEKRT LAGLTRQSDG AFDDTELVKI LQESIEDVAG AFGPNHVPAC MRAIEILGIK
QSRTWNVATL NEFRQFIGLT PHDSFYHMNP DPKICKILAQ MYDSPDAVEL YPGIMAEAAK
PPFSPGSGLC PPYTTSRAIL SDAVSLVRGD RFYTVDYTPR NITNWGFNEA STDKAVDWGH
VIYKLFFRAF PNHFLPNSVY AHFPFVVPSE NKLIFEGLGA ANKYSWDPPK ARAPIQFIRS
HKAVLEVLSN QKDYKVTWGP AIKMLSGDPA TSFALAGDEP ANAASRHHVI AALTAPKQWR
DEVRRFYEVT TRDLLRRHGA PVHGVGAGPR THEVDVIRDV IGLAHARFMA SLFSLPLKEE
GKEEGAYGEH ELYRSLVTIF AAIFWDSDVC NSLKLHQASK AAADKMSALI AEHVREMEAG
TGFLGALGKL KDLITGNDVH ANGNGVYTNG NGVYTNGNGV HTNGNGVHTN GNGVPHAAPS
LRSFGDQLLQ RMLSQDGRSI EETVSGTILP VVMAGTANQT QLLAQCLDYY LGVGEKHLPE
MKRLAMLNTS EADEKLLKYT MEGCRIRGCV ALYRAVVTDQ AVDDTIPCIP NKDDPTFARP
LSNPQVAESA RTLKLSTGTR MLVDLTTASH DPAAFPDPDE VRLDRPLESY VHFGLGPHRC
AGEPISQIAL SSVMKVLLQL DGLRRAAGPR GEIRSYPASQ WPGQAGRPPR DPAWSGLRTF
TSADQSAFSP LATTMKINWE GRGDL
//
