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

AJ507212; CAD45186.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P08170; 2SBL. [HSSP ENTRY / PDB]

ModBase

Q8GSM3.

Organism-specific databases

Gramene

Q8GSM3; -.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
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

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`	`? 932`		`Lipoxygenase 2.2, chloroplastic.`	`PRO_0000018324`
`DOMAIN`	`79 219`	`141`	`PLAT.`
`DOMAIN`	`223 932`	`710`	`Lipoxygenase.`
`METAL`	`588 588`		`Iron; catalytic (By similarity).`
`METAL`	`593 593`		`Iron; catalytic (By similarity).`
`METAL`	`778 778`		`Iron; catalytic (By similarity).`
`METAL`	`782 782`		`Iron; catalytic (By similarity).`
`METAL`	`932 932`		`Iron; via carboxylate; catalytic (By similarity).`

Sequence information

Length: 932 AA [This is the length of the unprocessed precursor]

Molecular weight: 106493 Da [This is the MW of the unprocessed precursor]

CRC64: 64D80DF4370F30E0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQTATKPLVG ARAVPLSRRA SFLVAEARRK PSTNARRTRV GSTSTTTTTT TILTDVNGPA 

        70         80         90        100        110        120 
LTTVAKPGHQ YDLKQTVEMK ATVSVHMKSF WWSDEKKERA RDWAYDLILG SWLTLELVSS 

       130        140        150        160        170        180 
ELDPKTGQEH DVISGKLKHS RETEKDYDLY EAIFTCRHRL APSGAVRLVN YHHTEMLLGE 

       190        200        210        220        230        240 
VKIFPAGEDP TKSSAVTLFH CQSWIDPSHC SPDKRTFFPV EKSYIPSQTP KGVEKLRKSE 

       250        260        270        280        290        300 
LEALRGNGCG ERKKHDRIYD YDVYNDLGKP ESKRPVLGGK EHPYPRRCRT GRPRSKTDPS 

       310        320        330        340        350        360 
SEEESHKKGE MYVPRDETFT ERKEQAFLTK QLLSQLHGLC TGLKVNKDIL PSFPTLASID 

       370        380        390        400        410        420 
ALYDDDFRNQ PVQPEGGKVR LILDLLAKEL VHLVKLEGAE FVEGIRRVFK FETPEIHDMD 

       430        440        450        460        470        480 
KLAWFRDEEF ARQTLAGMNP LSIQLVTELP IVSKLDELKY GPADSLITKE LIEKQINRIM 

       490        500        510        520        530        540 
TAEEAVAQKK LFMLDYHDLL LPYVHRVRKL DNKTMYGSRT LFFLADDGTL RPIAIELTRP 

       550        560        570        580        590        600 
KSPHKQQWRK VFTPGSGYSG SVTGSWEWQL AKIHVLSHDT GYHQLVSHWL RTHCCVEPYV 

       610        620        630        640        650        660 
IAANRQLSQM HPIYRLLHPH FRFTMEINAQ ARGMLICADG IIEKTFSPGE FSMEISSAAY 

       670        680        690        700        710        720 
DKQWRFDMEA LPEDLIRRGM AVRGEDGKLE LAIEDYPYAN DGLLVWDAIK QWASDYVAHY 

       730        740        750        760        770        780 
YPCAVDIVDD EELQDWWTEV RTKGHPDKQD EPWWPELDCH ESLVQVLATI MWVTSAHHAA 

       790        800        810        820        830        840 
VNFGQYPMAG YVPNHPSIAR RNMPCEMGPE EMLAFKAAPE KVWLDTLPSQ LQTVMVMATL 

       850        860        870        880        890        900 
DLLSSHASDE EYMGTHQEPA WQRDGEVDKA FQVFQKKMRD IAEQVEEWNK DDSRRNRHGA 

       910        920        930 
GVVPYVLLRP LNGNPMDAKT VMEMGIPNSI SI

Q8GSM3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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