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UniProtKB/Swiss-Prot entry Q9UUS2

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LIDS_GAEGR
Primary accession number Q9UUS2
Secondary accession numbers None
Integrated into Swiss-Prot on February 11, 2002
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 45)
Name and origin of the protein
Protein name Linoleate diol synthase
Synonyms EC 1.13.11.44
Linoleate (8R)-dioxygenase
Linoleate 8-dioxygenase
Gene name None
From
Gaeumannomyces graminis var. graminis [TaxID: 36780] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Sordariomycetes incertae sedis; Magnaporthaceae; Gaeumannomyces.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=DAR 23471;
DOI=10.1074/jbc.274.40.28219; PubMed=10497176 [NCBI, ExPASy, EBI, Israel, Japan]
Hoernsten L., Su C., Osbourn A.E., Garosi P., Hellman U., Wernstedt C., Oliw E.H.;
"Cloning of linoleate diol synthase reveals homology with prostaglandin H synthases.";
J. Biol. Chem. 274:28219-28224(1999).
[2]
 CHARACTERIZATION.
DOI=10.1074/jbc.271.24.14112; PubMed=8662736 [NCBI, ExPASy, EBI, Israel, Japan]
Su C., Oliw E.H.;
"Purification and characterization of linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as a novel hemoprotein.";
J. Biol. Chem. 271:14112-14118(1996).
Comments
  • FUNCTION: Catalyzes the dioxygenation of linoleic acid to (8R)-hydroperoxylinoleate and isomerization of the resulting hydroperoxide to (7S,8S)-dihydroxylinoleate.
  • CATALYTIC ACTIVITY: Linoleate + O2 = (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate.
  • COFACTOR: Heme group.
  • SUBUNIT: Homotetramer.
  • PTM: The N-terminus is blocked.
  • SIMILARITY: Belongs to the peroxidase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF124979; AAD49559.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase Q9UUS2.
Protein family/group databases
PeroxiBase 4150; GgrLDS.
Ontologies
GO
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0033751; Molecular function: linoleate diol synthase activity (inferred from electronic annotation from EC).
GO:0004497; Molecular function: monooxygenase activity (inferred from electronic annotation from InterPro).
GO:0004601; Molecular function: peroxidase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979; Biological process: response to oxidative stress (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002007; Haem_peroxidase_animal.
Graphical view of domain structure.
Gene3D G3DSA:1.10.640.10; Haem_peroxidase_animal; 1.
Pfam PF03098; An_peroxidase; 1.
Pfam graphical view of domain structure.
PRINTS PR00457; ANPEROXIDASE.
PROSITE PS50292; PEROXIDASE_3; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9UUS2.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Dioxygenase; Direct protein sequencing; Heme; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   978  978     Linoleate diol synthase. PRO_0000055599
ACT_SITE   376   376        Potential. 
METAL   203   203        Iron (heme axial ligand) (Potential). 
METAL   379   379        Iron (heme axial ligand) (Potential). 
Sequence information
Length: 978 AA [This is the length of the unprocessed precursor] Molecular weight: 107965 Da [This is the MW of the unprocessed precursor] CRC64: 104CC8541740ED3D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTVSTHHDDS PGLSGRLRDL LHHVFGNQKS PTVYPNAPGN SAKPVPTGLA DDIDKLGFKD 

        70         80         90        100        110        120 
IDTLLIFLNS AVKGVNDDQQ FLLEKMIQLL AKLPPASREG KKLTDGLIND LWDSLDHPPV 

       130        140        150        160        170        180 
ASLGKGFSFR EPDGSNNNIH LPSLGAANTP YARSTKPLVF QNPNPPDPAT IFDTLMVRDP 

       190        200        210        220        230        240 
AKFRPHPNKI SSMLFYLATI ITHDIFQTSP RDFNINLTSS YLDLSPLYGR NHDEQMAVRT 

       250        260        270        280        290        300 
GKDGLLKPDT FSSKRVIGFP PGVGAFLIMF NRFHNYVVTQ LAKINEGGRF KRPTTPDDTA 

       310        320        330        340        350        360 
GWETYDNSLF QTGRLITCGL YINIVLGDYV RTILNLNRAN TTWNLDPRTK EGKSLLSKPT 

       370        380        390        400        410        420 
PEAVGNQVSV EFNLIYRWHC TISERDDKWT TNAMREALGG QDPATAKMED VMRALGMFEK 

       430        440        450        460        470        480 
NIPDEPEKRT LAGLTRQSDG AFDDTELVKI LQESIEDVAG AFGPNHVPAC MRAIEILGIK 

       490        500        510        520        530        540 
QSRTWNVATL NEFRQFIGLT PHDSFYHMNP DPKICKILAQ MYDSPDAVEL YPGIMAEAAK 

       550        560        570        580        590        600 
PPFSPGSGLC PPYTTSRAIL SDAVSLVRGD RFYTVDYTPR NITNWGFNEA STDKAVDWGH 

       610        620        630        640        650        660 
VIYKLFFRAF PNHFLPNSVY AHFPFVVPSE NKLIFEGLGA ANKYSWDPPK ARAPIQFIRS 

       670        680        690        700        710        720 
HKAVLEVLSN QKDYKVTWGP AIKMLSGDPA TSFALAGDEP ANAASRHHVI AALTAPKQWR 

       730        740        750        760        770        780 
DEVRRFYEVT TRDLLRRHGA PVHGVGAGPR THEVDVIRDV IGLAHARFMA SLFSLPLKEE 

       790        800        810        820        830        840 
GKEEGAYGEH ELYRSLVTIF AAIFWDSDVC NSLKLHQASK AAADKMSALI AEHVREMEAG 

       850        860        870        880        890        900 
TGFLGALGKL KDLITGNDVH ANGNGVYTNG NGVYTNGNGV HTNGNGVHTN GNGVPHAAPS 

       910        920        930        940        950        960 
LRSFGDQLLQ RMLSQDGRSI EETVSGTILP VVMAGTANQT QLLAQCLDYY LGVGEKHLPE 

       970 
MKRLAMLNTS EADEKLLK
Q9UUS2 in FASTA format

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