NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 213-227, CATALYTIC ACTIVITY, FUNCTION, AND INDUCTION.
STRAIN=cv. Salome;
TISSUE=Leaf;
PubMed=9492266 [NCBI, ExPASy, EBI, Israel, Japan]
Voeroes K., Feussner I., Kuehn H., Lee J., Graner A., Loebler M., Parthier B., Wasternack C.;
"Characterization of a methyljasmonate-inducible lipoxygenase from barley (Hordeum vulgare cv. Salome) leaves.";
Eur. J. Biochem. 251:36-44(1998).

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 is possibly involved in jasmonic acid synthesis. It exhibits linoleate 13-lipoxygenase and arachidonate 15-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).
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 7;
PATHWAY: Lipid metabolism; oxylipin biosynthesis .
SUBCELLULAR LOCATION: Plastid, chloroplast.
INDUCTION: Transient induction by exogenous methyl jasmonate, reaching a maximum 48 hours after treatment. Not induced by endogenous jasmonic acid resulting from sorbitol stress.
PTM: The N-terminus is blocked.
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

U56406; AAC12951.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T06190; T06190.

3D structure databases

HSSP

P08170; 2SBL. [HSSP ENTRY / PDB]

ModBase

P93184.

Organism-specific databases

Gramene

P93184; -.

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; Direct protein sequencing; 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`	`? 936`		`Lipoxygenase 2.1, chloroplastic.`	`PRO_0000018323`
`DOMAIN`	`88 217`	`130`	`PLAT.`
`DOMAIN`	`220 936`	`717`	`Lipoxygenase.`
`METAL`	`587 587`		`Iron; catalytic (By similarity).`
`METAL`	`592 592`		`Iron; catalytic (By similarity).`
`METAL`	`777 777`		`Iron; catalytic (By similarity).`
`METAL`	`781 781`		`Iron; catalytic (By similarity).`
`METAL`	`936 936`		`Iron; via carboxylate; catalytic (By similarity).`

Sequence information

Length: 936 AA [This is the length of the unprocessed precursor]

Molecular weight: 105864 Da [This is the MW of the unprocessed precursor]

CRC64: 567B8519E0B5D959 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLTATKPLVG GACAAPSSSA RRRTFVVPEA RRKPGNGRRT SVSKVGSTST STTTTTTTTL 

        70         80         90        100        110        120 
SADSNGAAVG TVTRPDVHVQ DRTHATEMKA TVTVHMSKAA GVRDFLYDLI LKTWLHVDLV 

       130        140        150        160        170        180 
SSELDPQTGQ EREPISGAVK HSGRVDDEWD MYEATFKVPA SFGPIGAVQV TNYHHSEMLL 

       190        200        210        220        230        240 
GDIEVFPTGQ EESAVTFHCK SWIDPSHCTP DKRVFFPAHS YLPSQTPKGV EGLRKRELEI 

       250        260        270        280        290        300 
LRGTGCGERK EHDRIYDYDV YNDLGNPDDD NNPTTRPVLG GKEHPYPRRC RTGRPRSKKD 

       310        320        330        340        350        360 
PFSEERSHKE HIYVPRDEAF TERKMGAFDT KKFMSQLHAL TTGLKTAKHK SQSFPSLSAI 

       370        380        390        400        410        420 
DQLYDDNFRN QPVQPEGGKL RFVIDLLETE LLHLFKLEGA AFLEGIRRVF KFETPEIHDR 

       430        440        450        460        470        480 
DKFAWFRDEE FARQTIAGMN PMSIQLVTEF PIKSNLDEAT YGPADSLITK EVVEEQIRRV 

       490        500        510        520        530        540 
MTADEAVQNK KLFMLDYHDL LLPYVHKVRK LDGTTLYGSR ALFFLTADGT LRPIAIELTR 

       550        560        570        580        590        600 
PKSKKKPQWR QVFTPGCDGS VTGSWLWQLA KAHILAHDAG VHQLVSHWLR THACTEPYII 

       610        620        630        640        650        660 
AANRQLSQMH PVYRLLHPHF RFTMEINAQA RAMLINAGGI IEGSFVPGEY SLELSSVAYD 

       670        680        690        700        710        720 
QQWRFDMEAL PEDLIRRGMA VRNPNGELEL AIEDYPYAND GLLVWDAIKQ WALTYVQHYY 

       730        740        750        760        770        780 
PCAADIVDDE ELQAWWTEVR TKGHADKQDE PWWPELDSHE NLAQTLATIM WVTSGHHAAV 

       790        800        810        820        830        840 
NFGQYPMAGY IPNRPTMARR NMPTEIGGDD MRDFVEAPEK VLLDTFPSQY QSAIVLAILD 

       850        860        870        880        890        900 
LLSTHSSDEE YMGTHEEPAW TKDGVINQAF EEFKESTRKI VEQVDEWNND PDRKNRHGAG 

       910        920        930 
MVPYVLLRPS DGDPTDGDPT DEKMVMEMGI PNSISI

P93184 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