Q9UUS2 (LIDS_GAEGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Linoleate diol synthase EC=1.13.11.44 Alternative name(s): Linoleate (8R)-dioxygenase Short name=Linoleate 8-dioxygenase
Organism	Gaeumannomyces graminis var. graminis
Taxonomic identifier	36780 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Magnaporthales › Magnaporthaceae › Gaeumannomyces

Protein attributes

Sequence length	1165 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	Heme Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase Peroxidase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	response to oxidative stress Inferred from electronic annotation. Source: InterPro
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro linoleate diol synthase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Inferred from electronic annotation. Source: InterPro peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1165	1165	Linoleate diol synthase		PRO_0000055599
Sites
	Active site	376	1	Potential
	Metal binding	203	1	Iron (heme axial ligand) Potential
	Metal binding	379	1	Iron (heme axial ligand) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9UUS2 [UniParc]. Last modified July 13, 2010. Version 3. Checksum: 03D0B4170F56E452	FASTA	1,165	128,322
	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 970 980 990 1000 1010 1020 MKRLAMLNTS EADEKLLKYT MEGCRIRGCV ALYRAVVTDQ AVDDTIPCIP NKDDPTFARP 1030 1040 1050 1060 1070 1080 LSNPQVAESA RTLKLSTGTR MLVDLTTASH DPAAFPDPDE VRLDRPLESY VHFGLGPHRC 1090 1100 1110 1120 1130 1140 AGEPISQIAL SSVMKVLLQL DGLRRAAGPR GEIRSYPASQ WPGQAGRPPR DPAWSGLRTF 1150 1160 TSADQSAFSP LATTMKINWE GRGDL

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
EMBL GenBank DDBJ	AF124979 Genomic DNA. Translation: AAD49559.3.
3D structure databases
ModBase	Search...
Protein family/group databases
PeroxiBase	4150. GgrLDS.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR010255. Haem_peroxidase. IPR002007. Haem_peroxidase_animal. IPR019791. Haem_peroxidase_animal_subgr. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 2 hits. G3DSA:1.10.640.10. Haem_peroxidase_animal. 1 hit.
Pfam	PF03098. An_peroxidase. 1 hit. PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00457. ANPEROXIDASE.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit. SSF48113. Peroxidase_super. 1 hit.
PROSITE	PS50292. PEROXIDASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LIDS_GAEGR

Accession

Primary (citable) accession number: Q9UUS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 11, 2002
Last sequence update:	July 13, 2010
Last modified:	June 28, 2011
This is version 60 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program