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Reviewed, UniProtKB/Swiss-Prot P24095 (LOXX_SOYBN)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    Seed lipoxygenase
    EC=1.13.11.12
Gene names
Name: LOX1.4
Synonyms: SC514
OrganismGlycine max (Soybean)
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Glycine

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Protein attributes

Sequence length864 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

Pathway

Lipid metabolism; oxylipin biosynthesis.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Tissue specificity

Germinated cotyledons.

Induction

By jasmonate.

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.

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Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
Oxylipin biosynthesis
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical term3D-structure
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 functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 864864Seed lipoxygenase
PRO_0000220721

Regions

Domain44 – 171128PLAT
Domain174 – 864691Lipoxygenase

Sites

Metal binding5251Iron; catalytic
Metal binding5301Iron; catalytic
Metal binding7161Iron; catalytic
Metal binding7201Iron; catalytic
Metal binding8641Iron; via carboxylate; catalytic

Experimental info

Sequence conflict2331S → C in AAA03728. Ref.2
Sequence conflict2401R → L in AAA03728. Ref.2
Sequence conflict6041D → H in AAA03728. Ref.2
Sequence conflict6951M → K in AAA03728. Ref.2

Secondary structure

1 .................................................................................................................................................. 864
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P24095-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 66F31FB1FA5F3B60

FASTA86496,817
        10         20         30         40         50         60 
MFGIFDKGQK IKGTVVLMPK NVLDFNAITS IGKGGVIDTA TGILGQGVSL VGGVIDTATS 

        70         80         90        100        110        120 
FLGRNISMQL ISATQTDGSG NGKVGKEVYL EKHLPTLPTL GARQDAFSIF FEWDASFGIP 

       130        140        150        160        170        180 
GAFYIKNFMT DEFFLVSVKL EDIPNHGTIE FVCNSWVYNF RSYKKNRIFF VNDTYLPSAT 

       190        200        210        220        230        240 
PAPLLKYRKE ELEVLRGDGT GKRKDFDRIY DYDVYNDLGN PDGGDPRPIL GGSSIYPYPR 

       250        260        270        280        290        300 
RVRTGRERTR TDPNSEKPGE VYVPRDENFG HLKSSDFLTY GIKSLSHDVI PLFKSAIFQL 

       310        320        330        340        350        360 
RVTSSEFESF EDVRSLYEGG IKLPTDILSQ ISPLPALKEI FRTDGENVLQ FPPPHVAKVS 

       370        380        390        400        410        420 
KSGWMTDEEF AREVIAGVNP NVIRRLQEFP PKSTLDPTLY GDQTSTITKE QLEINMGGVT 

       430        440        450        460        470        480 
VEEALSTQRL FILDYQDAFI PYLTRINSLP TAKAYATRTI LFLKDDGTLK PLAIELSKPH 

       490        500        510        520        530        540 
PDGDNLGPES IVVLPATEGV DSTIWLLAKA HVIVNDSGYH QLVSHWLNTH AVMEPFAIAT 

       550        560        570        580        590        600 
NRHLSVLHPI YKLLYPHYRD TININGLARQ SLINADGIIE KSFLPGKYSI EMSSSVYKNW 

       610        620        630        640        650        660 
VFTDQALPAD LVKRGLAIED PSAPHGLRLV IEDYPYAVDG LEIWDAIKTW VHEYVSLYYP 

       670        680        690        700        710        720 
TDAAVQQDTE LQAWWKEAVE KGHGDLKEKP WWPKMQTTED LIQSCSIIVW TASALHAAVN 

       730        740        750        760        770        780 
FGQYPYGGLI LNRPTLARRF IPAEGTPEYD EMVKNPQKAY LRTITPKFET LIDLSVIEIL 

       790        800        810        820        830        840 
SRHASDEIYL GERETPNWTT DKKALEAFKR FGSKLTGIEG KINARNSDPS LRNRTGPVQL 

       850        860 
PYTLLHRSSE EGLTFKGIPN SISI

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References

[1]"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].
Tissue: Cotyledon.
[2]Park T., Holland M.A., Laskey J.G., Polacco J.C.
Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Williams 82.
Tissue: Radicle.
[3]"Crystal structures of vegetative soybean lipoxygenase VLX-B and VLX-D, and comparisons with seed isoforms LOX-1 and LOX-3."
Youn B., Sellhorn G.E., Mirchel R.J., Gaffney B.J., Grimes H.D., Kang C.
Proteins 65:1008-1020(2006) [PubMed: 17022084] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON IONS.

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Cross-references

Sequence databases

X56139 Genomic DNA. Translation: CAA39604.1.
U04526 mRNA. Translation: AAA03728.1.
PIRS13381.
UniGeneGma.11166

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2IUKX-ray2.40A/B1-864[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.13.11.12. 299.

Family and domain databases

InterProIPR000907. LipOase.
IPR013819. LipOase_C.
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...

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Entry information

Entry nameLOXX_SOYBN
AccessionPrimary (citable) accession number: P24095
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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