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Reviewed, UniProtKB/Swiss-Prot P27480 (LOXA_PHAVU)

Last modified February 9, 2010. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lipoxygenase 1
    EC=1.13.11.12
Gene names
Name: LOXA
Synonyms: LOX1
OrganismPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifier3885 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

Protein attributes

Sequence length862 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (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 structure

Monomer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
Oxylipin biosynthesis
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

oxylipin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 862862Lipoxygenase 1
PRO_0000220715

Regions

Domain44 – 171128PLAT
Domain174 – 862689Lipoxygenase

Sites

Metal binding5221Iron; catalytic By similarity
Metal binding5271Iron; catalytic By similarity
Metal binding7131Iron; catalytic By similarity
Metal binding7171Iron; catalytic By similarity
Metal binding8621Iron; via carboxylate; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
P27480-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 24D56D1CEE3C191E

FASTA86297,155
        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 

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References

[1]"Complex spatial and temporal expression of lipoxygenase genes during Phaseolus vulgaris (L.) development."
Eiben H.G., Slusarenko A.J.
Plant J. 5:123-135(1994) [PubMed: 8130796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Red Mexican.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63525 Genomic DNA. Translation: CAA45088.1.
PIRS22153.

3D structure databases

SMRP27480. Positions 8-862.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.13.11.12. 8.

Family and domain databases

InterProIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001024. LipOase_LH2.
IPR001246. LipOase_pln.
[Graphical view]
Gene3DG3DSA:2.60.60.20. Lipase_LipOase. 1 hit.
PANTHERPTHR11771. LipOase. 1 hit.
PfamPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLOXA_PHAVU
AccessionPrimary (citable) accession number: P27480
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: February 9, 2010
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents