NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
STRAIN=cv. Salome;
TISSUE=Leaf;
PubMed=12452441 [NCBI, ExPASy, EBI, Israel, Japan]
Bachmann A., Hause B., Maucher H., Garbe E., Voeroes K., Weichert H., Wasternack C., Feussner I.;
"Jasmonate-induced lipid peroxidation in barley leaves initiated by distinct 13-LOX forms of the chloroplast.";
Biol. Chem. 383:1645-1657(2002).

Comments

FUNCTION: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. This enzyme exhibits linoleate 13-lipoxygenase activity.
CATALYTIC ACTIVITY: Linoleate + O₂ = (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate.
COFACTOR: Binds 1 iron ion per subunit. Iron is tightly bound (By similarity).
PATHWAY: Lipid metabolism; oxylipin biosynthesis .
SUBCELLULAR LOCATION: Plastid, chloroplast.
SIMILARITY: Belongs to the lipoxygenase family.
SIMILARITY: Contains 1 lipoxygenase domain.
SIMILARITY: Contains 1 PLAT domain.

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

AJ507213; CAD45187.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P08170; 2SBL. [HSSP ENTRY / PDB]

ModBase

Q8GSM2.

Organism-specific databases

Gramene

Q8GSM2; -.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0016165;	Molecular function: lipoxygenase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0031408;	Biological process: oxylipin biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000907; LipOase.
IPR013819; LipOase_C.
IPR001024; LipOase_LH2.
IPR001246; LipOase_pln.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.60.20; Lipase_LipOase; 1.

PANTHER

PTHR11771; LipOase; 1.

Pfam

PF00305; Lipoxygenase; 1.
PF01477; PLAT; 1.
Pfam graphical view of domain structure.

PRINTS

PR00087; LIPOXYGENASE.
PR00468; PLTLPOXGNASE.

SMART

SM00308; LH2; 1.
SMART graphical view of domain structure.

PROSITE

PS00711; LIPOXYGENASE_1; 1.
PS00081; LIPOXYGENASE_2; 1.
PS51393; LIPOXYGENASE_3; 1.
PS50095; PLAT; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

Q8GSM2.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Chloroplast; Dioxygenase; Fatty acid biosynthesis; Iron; Lipid synthesis; Metal-binding; Oxidoreductase; Oxylipin biosynthesis; Plastid; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Chloroplast (Potential).`
`CHAIN`	`? 896`		`Lipoxygenase 2.3, chloroplastic.`	`PRO_0000018325`
`DOMAIN`	`80 199`	`120`	`PLAT.`
`DOMAIN`	`202 896`	`695`	`Lipoxygenase.`
`METAL`	`556 556`		`Iron; catalytic (By similarity).`
`METAL`	`561 561`		`Iron; catalytic (By similarity).`
`METAL`	`746 746`		`Iron; catalytic (By similarity).`
`METAL`	`750 750`		`Iron; catalytic (By similarity).`
`METAL`	`896 896`		`Iron; via carboxylate; catalytic (By similarity).`

Sequence information

Length: 896 AA [This is the length of the unprocessed precursor]

Molecular weight: 101234 Da [This is the MW of the unprocessed precursor]

CRC64: 31511189946B866A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIHLKQPLVL SAQSSNVASP LFVAGGQQRR ASGAGRTCSG RRLSARRISC ASTEEAVGVS 

        70         80         90        100        110        120 
TSVTTKERAL TVTAIVTAQV PTSVYVARGL DDIQDLFGKT LLLELVSSEL DPKTGRERER 

       130        140        150        160        170        180 
VKGFAHMTLK EGTYEAKMSV PASFGPVGAV LVENEHHREM FIKDIKLITG GDESTAITFD 

       190        200        210        220        230        240 
VASWVHSKFD DPEPRAFFTV KSYLPSQTPP GIEALRKKEL ETLRGDGHSE RKFHERVYDY 

       250        260        270        280        290        300 
DTYNDLGDPD KNIDHKRPVL GTKEHPYPRR CRTGRPKTLY DPETETRSSP VYVPRDEQFS 

       310        320        330        340        350        360 
DVKGRTFSAT TLRSGLHAIL PAVAPLLNNS HGFSHFPAID ALYSDGIPLP VDGHGGNSFN 

       370        380        390        400        410        420 
VINDVIPRVV QMIEDTTEHV LRFEVPEMLE RDRFSWFRDE EFARQTLAGL NPICIRRLTE 

       430        440        450        460        470        480 
FPIVSKLDPA VYGPAESALS KEILEKMMNG RMTVEEAMEK KRLFLLDYHD VFLPYVHRVR 

       490        500        510        520        530        540 
ELPDTTLYGS RTVFFLSDEG TLMPLAIELT RPQSPTKPQW KRAFTHGSDA TESWLWKLAK 

       550        560        570        580        590        600 
AHVLTHDTGY HQLVSHWLRT HACVEPYIIA TNRQLSRMHP VYRLLHPHFR YTMEINALAR 

       610        620        630        640        650        660 
EALINADGII EEAFLAGKYS IELSSVAYGA AWQFNTEALP EDLINRGLAV RRDDGELELA 

       670        680        690        700        710        720 
IKDYPYADDG LLIWGSIKQW ASDYVDFYYK SDGDVAGDEE LRAWWEEVRT KGHADKKDEP 

       730        740        750        760        770        780 
WWPVCDTKEN LVQILTIIMW VTSGHHAAVN FGQYHYAGYF PNRPTVVRRN IPVEENRDDE 

       790        800        810        820        830        840 
MKKFMARPEE VLLQSLPSQM QAIKVMATLD ILSSHSPDEE YMGEYAEPAW LAEPMVKAAF 

       850        860        870        880        890 
EKFSGRLKEA EGTIDMRNNN PENKNRCGAG IVPYELLKPF SEPGVTGRGI PNSISI

Q8GSM2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools