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Reviewed, UniProtKB/Swiss-Prot Q9UUS2 (LIDS_GAEGR)

Last modified May 26, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Linoleate diol synthase
    EC=1.13.11.44
Alternative name(s):
    Linoleate (8R)-dioxygenase
      Short name=Linoleate 8-dioxygenase
OrganismGaeumannomyces graminis var. graminis
Taxonomic identifier36780 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeMagnaporthalesMagnaporthaceaeGaeumannomyces

Protein attributes

Sequence length978 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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 structure

Homotetramer.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the peroxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 978978Linoleate diol synthase
PRO_0000055599

Sites

Active site3761 Potential
Metal binding2031Iron (heme axial ligand) Potential
Metal binding3791Iron (heme axial ligand) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9UUS2-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 104CC8541740ED3D

FASTA978107,965
        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 

« Hide

References

[1]"Cloning of linoleate diol synthase reveals homology with prostaglandin H synthases."
Hoernsten L., Su C., Osbourn A.E., Garosi P., Hellman U., Wernstedt C., Oliw E.H.
J. Biol. Chem. 274:28219-28224(1999) [PubMed: 10497176] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: DAR 23471.
[2]"Purification and characterization of linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as a novel hemoprotein."
Su C., Oliw E.H.
J. Biol. Chem. 271:14112-14118(1996) [PubMed: 8662736] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

AF124979 Genomic DNA. Translation: AAD49559.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

PeroxiBase4150. GgrLDS.

Enzyme and pathway databases

BRENDA1.13.11.44. 189161.

Family and domain databases

InterProIPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_sg.
[Graphical view]
Gene3DG3DSA:1.10.640.10. Haem_peroxidase_animal. 1 hit.
PfamPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
PROSITEPS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLIDS_GAEGR
AccessionPrimary (citable) accession number: Q9UUS2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: May 1, 2000
Last modified: May 26, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents