NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Caruso;
TISSUE=Pericarp;
DOI=10.1104/pp.106.1.109; PubMed=7972514 [NCBI, ExPASy, EBI, Israel, Japan]
Ferrie B.J., Beaudoin N., Burkhart W., Bowsher C.G., Rothstein S.J.;
"The cloning of two tomato lipoxygenase genes and their differential expression during fruit ripening.";
Plant Physiol. 106:109-118(1994).

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 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Expressed in germinating seeds as well as in ripening fruit.
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

U09026; AAA53184.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Les.3668

3D structure databases

HSSP

P08170; 1FGT. [HSSP ENTRY / PDB]

ModBase

P38415.

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

Cytoplasm; Dioxygenase; Fatty acid biosynthesis; Iron; Lipid synthesis; Metal-binding; Oxidoreductase; Oxylipin biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 860`	`860`	`Lipoxygenase A.`	`PRO_0000220705`
`DOMAIN`	`29 159`	`131`	`PLAT.`
`DOMAIN`	`162 860`	`699`	`Lipoxygenase.`
`METAL`	`521 521`		`Iron; catalytic (By similarity).`
`METAL`	`526 526`		`Iron; catalytic (By similarity).`
`METAL`	`712 712`		`Iron; catalytic (By similarity).`
`METAL`	`716 716`		`Iron; catalytic (By similarity).`
`METAL`	`860 860`		`Iron; via carboxylate; catalytic (By similarity).`

Sequence information

Length: 860 AA [This is the length of the unprocessed precursor]

Molecular weight: 96765 Da [This is the MW of the unprocessed precursor]

CRC64: 43D1091853469426 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLGQLVGGLI GGHHDSKKVK GTVVMMKKNA LDFTDLAGSL TDKIFEALGQ KVSFQLISSV 

        70         80         90        100        110        120 
QSDPANGLQG KHSNPAYLEN FLLTLTPLAA GETAFGVTFD WNEEFGVPGA FVIKNMHINE 

       130        140        150        160        170        180 
FFLKSLTLED VPNHGKVHFV CNSWVYPSFR YKSDRIFFAN QPYLPSETPE LLRKYRENEL 

       190        200        210        220        230        240 
VTLRGDGTGK REAWDRIYDY DVYNDLGNPD QGKENVRTTL GGSADYPYPR RGRTGRPPTR 

       250        260        270        280        290        300 
TDPKSESRIP LILSLDIYVP RDERFGHLKM SDFLTYALKS IVQFILPELH ALFDGTPNEF 

       310        320        330        340        350        360 
DSFEDVLRLY EGGIKLPQGP LFKALTDAIP LEMIRELLRT DGEGILRFPT PLVIKDSKTA 

       370        380        390        400        410        420 
WRTDEEFARE MLAGVNPVII SRLEEFPPKS KLDPELYGNQ NSTITAEHIE GKLDGLTIDE 

       430        440        450        460        470        480 
AINSNKLFIL NHHDVLIPYL RRINTTTTKT YASRTLLFLQ DNGSLKPLAI ELSLPHPDGD 

       490        500        510        520        530        540 
QFGVTSKVYT PSDQGVEGSI WQLAKAYVAV NDSGVHQLIS HWLNTHAVIE PFVIATNRQL 

       550        560        570        580        590        600 
SVLHPIHKLL YPHFRDTMNI NALARQILIN AGGVLESTVF PSKFAMEMSA VVYKDWVFPD 

       610        620        630        640        650        660 
QALPADLVKR GVAVEDSSSP HGVRLLIDDY PYAVDGLEIW SAIKSWVTDY CSFYYGSNEE 

       670        680        690        700        710        720 
ILKDNELQAW WKEVREVGHG DKKNEPWWAE METPQELIDS CTTIIWIASA LHAAVNFGQY 

       730        740        750        760        770        780 
PYAGYLPNRP TVSRKFMPEP GTPEYEELKK NPDKAFLKTI TAQLQTLLGV SLIEILSRHT 

       790        800        810        820        830        840 
TDEIYLGQRE SPEWTKDKEP LAAFERFGNK LTDIEKQIMQ RNGNNILTNR TGPVNAPYTL 

       850        860 
LFPTSEGGLT GKGIPNSVSI

P38415 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