[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Red Mexican; TISSUE=Leaf; PubMed=8130796 [NCBI, ExPASy, EBI, Israel, Japan] Eiben H.G., Slusarenko A.J.; "Complex spatial and temporal expression of lipoxygenase genes during Phaseolus vulgaris (L.) development."; Plant J. 5:123-135(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.
SUBCELLULAR LOCATION: Cytoplasm.
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

X63525; CAA45088.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S22153; S22153.

3D structure databases

HSSP

P08170; 1F8N. [HSSP ENTRY / PDB]

ModBase

P27480.

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`	`1 862`	`862`	`Lipoxygenase 1.`	`PRO_0000220715`
`DOMAIN`	`44 171`	`128`	`PLAT.`
`DOMAIN`	`174 862`	`689`	`Lipoxygenase.`
`METAL`	`522 522`		`Iron; catalytic (By similarity).`
`METAL`	`527 527`		`Iron; catalytic (By similarity).`
`METAL`	`713 713`		`Iron; catalytic (By similarity).`
`METAL`	`717 717`		`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: 97155 Da [This is the MW of the unprocessed precursor]

CRC64: 24D56D1CEE3C191E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFGILNRGHK IKGTVVLMTK NVFDFNEFVS TTRGGIVGAA GGLFGAATDI VGGIVDGATA 

        70         80         90        100        110        120 
IFSRNIAIQL ISATKTDGLG NGKVGKQTFL EKHLPSLPNL GDRQDAFNVY FEWDENFGIP 

       130        140        150        160        170        180 
EAFYIKNFMQ SEFFLVSLTL EDIPNHGTIH FVCNSWVYNA KSYKRDRIFF ANKTYLPNET 

       190        200        210        220        230        240 
PASLVKYRKE ELENLRGDGT GERKEYDRIY DYAVYNDLGN PDKNKNLART TLGGSSDFPY 

       250        260        270        280        290        300 
PRRGRTGRKS TRKDPKCEIP TSDTYIPRDE NFGHLKSGDF LTYAIKSLTQ NVLPTFQKAF 

       310        320        330        340        350        360 
GFNNEFDTFE DVRGLFEGGL YLPTDVISKI SPIPVLKEIL RTDGEQVLKF PPPHVIRVTK 

       370        380        390        400        410        420 
SAWMTDEEFG REMLAGVNPC LIQRLQEFPP KSKLDVTVYG DQTSTMTKEH LEINLGGLTV 

       430        440        450        460        470        480 
EEALHGNRLF ILDHHDAFIP YLERINDLPT AKCYATRTIL FLKDDNTLKP LAIELSLPNP 

       490        500        510        520        530        540 
GGKGANSRVI LPADGGAEST IWLLAKAYVV VNDSCYHQLM SHWLNTHAVM EPFVIATNRH 

       550        560        570        580        590        600 
LSVLHPIYKL LLPHYRDTMN INALARQSLI NAGGVIERSF LPGEFAVEMS SAVYKSWVFT 

       610        620        630        640        650        660 
DQALPADLIK RGMAVEDPSS PYGLRLVVED YPYAVDGLEI WDTIQTWVKD YVSLYYPTND 

       670        680        690        700        710        720 
AVKKDTELQA WWKEAVEKGH GDLKDKPWWP KLNTPQDLIH TCSIIIWIAS ALHAAVNFGQ 

       730        740        750        760        770        780 
YPYGGFILNR PTITRRLLPE PGTKEYGELT SNYQKAYLRT ITGKVEAIVD LSVIEILSRH 

       790        800        810        820        830        840 
ASDEVYLGQR DNPNWTNNIK ALQAFKRFGQ KLKEIEEKIM GRNKDSSLRN RNGPVKMPYT 

       850        860 
VLLPTCEDEG LTFRGIPNSI SI

P27480 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