[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Triumph; DOI=10.1016/0005-2760(94)00231-M; PubMed=7827128 [NCBI, ExPASy, EBI, Israel, Japan] van Mechelen J.R., Smits M., Douma A.C., Rouster J., Cameron-Mills V., Heidekamp F., Valk B.E.; "Primary structure of a lipoxygenase from barley grain as deduced from its cDNA sequence."; Biochim. Biophys. Acta 1254:221-225(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 512-862. PubMed=14558691 [NCBI, ExPASy, EBI, Israel, Japan] Steiner-Lange S., Fischer A., Boettcher A., Rouhara I., Liedgens H., Schmelzer E., Knogge W.; "Differential defense reactions in leaf tissues of barley in response to infection by Rhynchosporium secalis and to treatment with a fungal avirulence gene product."; Mol. Plant Microbe Interact. 16:893-902(2003).
[3]	PROTEIN SEQUENCE OF 274-294 AND 832-845. STRAIN=cv. Triumph; TISSUE=Embryo; DOI=10.1016/0167-4838(92)90429-H; PubMed=1554746 [NCBI, ExPASy, EBI, Israel, Japan] Doderer A., Kokkelink I., van der Veen S., Valk B.E., Schram A.W., Douma A.C.; "Purification and characterization of two lipoxygenase isoenzymes from germinating barley."; Biochim. Biophys. Acta 1120:97-104(1992).

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. It catalyzes the hydroperoxidation of lipids, containing a cis,cis-1,4-pentadiene structure.
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 .
SUBUNIT: Monomer.
DEVELOPMENTAL STAGE: In both quiescent and germinating seeds.
MISCELLANEOUS: With linoleate as substrate, lipoxygenase 1 shows a specificity for carbon 9 as the site for hydroperoxidation (in contrast to lipoxygenase 2, which shows a preference for carbon 13).
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

L35931; AAA64893.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY220737; AAP04432.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S21772; S21772.
S22236; S22236.
T05941; T05941.

UniGene

Hv.9141

3D structure databases

HSSP

P08170; 1FGT. [HSSP ENTRY / PDB]

ModBase

P29114.

Organism-specific databases

Gramene

P29114; -.

Ontologies

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).

ProtoNet

P29114.

Other

UniRef

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

Keywords

Dioxygenase; Direct protein sequencing; Fatty acid biosynthesis; Iron; Lipid synthesis; Metal-binding; Oxidoreductase; Oxylipin biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 862`	`862`	`Lipoxygenase 1.`	`PRO_0000220723`
`DOMAIN`	`34 161`	`128`	`PLAT.`
`DOMAIN`	`164 862`	`699`	`Lipoxygenase.`
`METAL`	`517 517`		`Iron; catalytic (By similarity).`
`METAL`	`522 522`		`Iron; catalytic (By similarity).`
`METAL`	`708 708`		`Iron; catalytic (By similarity).`
`METAL`	`712 712`		`Iron; catalytic (By similarity).`
`METAL`	`862 862`		`Iron; via carboxylate; catalytic (By similarity).`

Sequence information

Length: 862 AA [This is the length of the unprocessed precursor]

Molecular weight: 96393 Da [This is the MW of the unprocessed precursor]

CRC64: F55954473467BEAA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLLGGLIDTL TGANKSARLK GTVVLMRKNV LDLNDFGATI IDGIGEFLGK GVTCQLISST 

        70         80         90        100        110        120 
AVDQDNGGRG KVGAEAELEQ WVTSLPSLTT GESKFGLTFD WEVEKLGVPG AIVVNNYHSS 

       130        140        150        160        170        180 
EFLLKTITLH DVPGRSGNLT FVANSWIYPA ANYRYSRVFF ANDTYLPSQM PAALKPYRDD 

       190        200        210        220        230        240 
ELRNLRGDDQ QGPYQEHDRI YRYDVYNDLG EGRPILGGNS DHPYPRRGRT ERKPNASDPS 

       250        260        270        280        290        300 
LESRLSLLEQ IYVPRDEKFG HLKTSDFLGY SIKAITQGIL PAVRTYVDTT PGEFDSFQDI 

       310        320        330        340        350        360 
INLYEGGIKL PKVAALEELR KQFPLQLIKD LLPVGGDSLL KLPVPHIIQE NKQAWRTDEE 

       370        380        390        400        410        420 
FAREVLAGVN PVMITRLTEF PPKSSLDPSK FGDHTSTITA EHIEKNLEGL TVQQALESNR 

       430        440        450        460        470        480 
LYILDHHDRF MPFLIDVNNL PGNFIYATRT LFFLRGDGRL TPLAIELSEP IIQGGLTTAK 

       490        500        510        520        530        540 
SKVYTPVPSG SVEGWVWELA KAYVAVNDSG WHQLVSHWLN THAVMEPFVI STNRHLSVTH 

       550        560        570        580        590        600 
PVHKLLSPHY RDTMTINALA RQTLINAGGI FEMTVFPGKF ALGMSAVVYK DWKFTEQGLP 

       610        620        630        640        650        660 
DDLIKRGMAV EDPSSPYKVR LLVSDYPYAA DGLAIWHAIE QYVSEYLAIY YPNDGVLQGD 

       670        680        690        700        710        720 
TEVQAWWKET REVGHGDLKD APWWPKMQSV PELAKACTTI IWIGSALHAA VNFGQYPYAG 

       730        740        750        760        770        780 
FLPNRPTVSR RRMPEPGTEE YAELERDPER AFIHTITSQI QTIIGVSLLE VLSKHSSDEL 

       790        800        810        820        830        840 
YLGQRDTPEW TSDPKALEVF KRFSDRLVEI ESKVVGMNHD PELKNRNGPA KFPYMLLYPN 

       850        860 
TSDHKGAAAG LTAKGIPNSI SI

P29114 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