GenomeNet

Database: UniProt/SWISS-PROT
Entry: LIDS_GAEGR
LinkDB: LIDS_GAEGR
Original site: LIDS_GAEGR 
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   22-NOV-2017, entry version 83.
DE   RecName: Full=Linoleate diol synthase;
DE            EC=1.13.11.60;
DE            EC=5.4.4.6;
DE   AltName: Full=Linoleate (8R)-dioxygenase;
DE            Short=Linoleate 8-dioxygenase;
OS   Gaeumannomyces graminis var. graminis (Turf grass take-all root rot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Magnaporthales; Magnaporthaceae;
OC   Gaeumannomyces.
OX   NCBI_TaxID=36780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=CBS 903.73;
RX   PubMed=10497176; DOI=10.1074/jbc.274.40.28219;
RA   Hoernsten L., Su C., Osbourn A.E., Garosi P., Hellman U.,
RA   Wernstedt C., Oliw E.H.;
RT   "Cloning of linoleate diol synthase reveals homology with
RT   prostaglandin H synthases.";
RL   J. Biol. Chem. 274:28219-28224(1999).
RN   [2]
RP   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: Catalyzes the dioxygenation of linoleic acid to (8R)-
CC       hydroperoxylinoleate and isomerization of the resulting
CC       hydroperoxide to (7S,8S)-dihydroxylinoleate.
CC   -!- CATALYTIC ACTIVITY: Linoleate + O(2) = (8R,9Z,12Z)-8-
CC       hydroperoxyoctadeca-9,12-dienoate. {ECO:0000269|PubMed:8662736}.
CC   -!- CATALYTIC ACTIVITY: (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-
CC       dienoate = (7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate.
CC       {ECO:0000269|PubMed:8662736}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000269|PubMed:8662736};
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.
CC       {ECO:0000255|PROSITE-ProRule:PRU00298}.
DR   EMBL; AF124979; AAD49559.3; -; Genomic_DNA.
DR   PeroxiBase; 4150; GgrLDS.
DR   PRIDE; Q9UUS2; -.
DR   KEGG; ag:AAD49559; -.
DR   KO; K17864; -.
DR   BRENDA; 1.13.11.60; 2376.
DR   BRENDA; 5.4.4.6; 2376.
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: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:0031408; P:oxylipin biosynthetic process; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd09817; linoleate_diol_synthase_like; 1.
DR   Gene3D; 1.10.630.10; -; 1.
DR   Gene3D; 1.10.640.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR010255; Haem_peroxidase.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR037120; Haem_peroxidase_sf.
DR   InterPro; IPR034807; Ppo.
DR   InterPro; IPR034812; Ppo_N.
DR   PANTHER; PTHR11903:SF13; PTHR11903:SF13; 1.
DR   Pfam; PF03098; An_peroxidase; 2.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 2.
DR   SUPFAM; SSF48264; SSF48264; 3.
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       Linoleate diol synthase.
FT                                /FTId=PRO_0000055599.
FT   ACT_SITE    376    376       {ECO:0000255}.
FT   METAL       203    203       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
FT   METAL       379    379       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
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
//
DBGET integrated database retrieval system