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Reviewed, UniProtKB/Swiss-Prot P09439 (LOX2_SOYBN)

Last modified February 9, 2010. Version 82. 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:
    Seed lipoxygenase-2
      Short name=L-2
    EC=1.13.11.12
Gene names
Name: LOX1.2
Synonyms: LOX2
OrganismGlycine max (Soybean)
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycine

Protein attributes

Sequence length865 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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.

Miscellaneous

Soybean contains at least 4 distinct isoenzymes, L-1, L-2, L-3a and L-3b in dry seeds, and at least two distinct isozymes in the hypocotyl/radicle region of the seedling stem.

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Sequence caution

The sequence described in Ref.2 differs from that shown. Reason: Frameshift at positions 691 and 865.

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 – 865865Seed lipoxygenase-2
PRO_0000220718

Regions

Domain50 – 175126PLAT
Domain178 – 865688Lipoxygenase

Sites

Metal binding5271Iron; catalytic By similarity
Metal binding5321Iron; catalytic By similarity
Metal binding7181Iron; catalytic By similarity
Metal binding7221Iron; catalytic By similarity
Metal binding8651Iron; via carboxylate; catalytic By similarity

Experimental info

Sequence conflict263 – 2642KP → NL Ref.2
Sequence conflict3131D → Y Ref.2
Sequence conflict4001L → P Ref.2
Sequence conflict4281L → H Ref.2
Sequence conflict4861D → G Ref.2
Sequence conflict5021V → G Ref.2
Sequence conflict5341V → L Ref.2

Sequences

Sequence LengthMass (Da)Tools
P09439-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 74CBD32E3E4A0C85

FASTA86597,146
        10         20         30         40         50         60 
MFSVPGVSGI LNRGGGHKIK GTVVLMRKNV LDFNSVADLT KGNVGGLIGT GLNVVGSTLD 

        70         80         90        100        110        120 
NLTAFLGRSV ALQLISATKP LANGKGKVGK DTFLEGIIVS LPTLGAGESA FNIQFEWDES 

       130        140        150        160        170        180 
MGIPGAFYIK NYMQVEFYLK SLTLEDVPNQ GTIRFVCNSW VYNTKLYKSV RIFFANHTYV 

       190        200        210        220        230        240 
PSETPAALVG YREEELKNLR GDGKGERKEH DRIYDYDVYN DLGNPDHGEN FARPILGGSS 

       250        260        270        280        290        300 
THPYPRRGRT GRYPTRKDQN SEKPGEVYVP RDENFGHLKS SDFLAYGIKS LSQYVLPAFE 

       310        320        330        340        350        360 
SVFDLNFTPN EFDSFQDVRD LHEGGIKLPT EVISTIMPLP VVKELFRTDG EQVLKFPPPH 

       370        380        390        400        410        420 
VIQVSKSAWM TDEEFAREMV AGVNPCVIRG LQEFPPKSNL DPTIYGEQTS KITADALDLD 

       430        440        450        460        470        480 
GYTVDEALAS RRLFMLDYHD VFMPYIRRIN QTYAKAYATR TILFLRENGT LKPVAIELSL 

       490        500        510        520        530        540 
PHPAGDLSGA VSQVILPAKE GVESTIWLLA KAYVVVNDSC YHQLMSHWLN THAVIEPFII 

       550        560        570        580        590        600 
ATNRHLSALH PIYKLLTPHY RDTMNINALA RQSLINADGI IEKSFLPSKH SVEMSSAVYK 

       610        620        630        640        650        660 
NWVFTDQALP ADLIKRGVAI KDPSAPHGLR LLIEDYPYAV DGLEIWAAIK TWVQEYVSLY 

       670        680        690        700        710        720 
YARDDDVKPD SELQQWWKEA VEKGHGDLKD KPWWPKLQTI EELVEICTII IWTASALHAA 

       730        740        750        760        770        780 
VNFGQYPYGG FILNRPTSSR RLLPEKGTPE YEEMVKSHQK AYLRTITSKF QTLVDLSVIE 

       790        800        810        820        830        840 
ILSRHASDEV YLGQRDNPHW TSDSKALQAF QKFGNKLKEI EEKLARKNND QSLSNRLGPV 

       850        860 
QLPYTLLHPN SEGLTCRGIP NSISI 

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References

[1]"Primary structure of soybean lipoxygenase L-2."
Shibata D., Steczko J., Dixon J.E., Andrews P.C., Hermodson M., Axelrod B.
J. Biol. Chem. 263:6816-6821(1988) [PubMed: 2834391] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Two soybean seed lipoxygenase nulls accumulate reduced levels of lipoxygenase transcripts."
Start W.G., Ma Y., Polacco J.C., Hildebrand D.F., Freyer G.A., Altschuler M.
Plant Mol. Biol. 7:11-23(1986) [Agricola: IND87003970]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-865.
[3]"Nucleotide sequences of a soybean lipoxygenase gene and the short intergenic region between an upstream lipoxygenase gene."
Shibata D., Kato T., Tanaka K.
Plant Mol. Biol. 16:353-359(1991) [PubMed: 1909908] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 859-865.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03211 mRNA. Translation: AAA33987.1.
X56139 Genomic DNA. Translation: CAA39605.1.
PIRDASYL1. A28161.

3D structure databases

SMRP09439. Positions 15-865.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.13.11.12. 299.

Gene expression databases

GenevestigatorP09439.

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 nameLOX2_SOYBN
AccessionPrimary (citable) accession number: P09439
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: February 9, 2010
This is version 82 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