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P09186 (LOX3_SOYBN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Seed linoleate 9S-lipoxygenase-3

EC=1.13.11.58
Alternative name(s):
Lipoxygenase-3
Short name=L-3
Gene names
Name:LOX1.3
Synonyms:LOX3
OrganismGlycine max (Soybean) (Glycine hispida) [Reference proteome]
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja

Protein attributes

Sequence length857 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate.

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 857857Seed linoleate 9S-lipoxygenase-3
PRO_0000220719

Regions

Domain38 – 163126PLAT
Domain166 – 857692Lipoxygenase

Sites

Metal binding5181Iron; catalytic
Metal binding5231Iron; catalytic
Metal binding7091Iron; catalytic
Metal binding7131Iron; catalytic
Metal binding8571Iron; via carboxylate; catalytic

Natural variations

Natural variant251H → D in strain: cv. Provar.
Natural variant571P → S in strain: cv. Provar.
Natural variant1121L → P in strain: cv. Provar.
Natural variant2011V → I in strain: cv. Provar.
Natural variant3821E → D in strain: cv. Provar.
Natural variant4281G → D in strain: cv. Provar.
Natural variant6301A → T in strain: cv. Provar.

Experimental info

Mutagenesis7131N → A or S: No loss of iron-binding; loss of catalytic activity. Ref.3
Mutagenesis7131N → H: No loss of iron-binding; no change in catalytic activity. Ref.3

Secondary structure

......................................................................................................................................................................... 857
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09186 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 5DFC33D0F6FD32F0

FASTA85796,758
        10         20         30         40         50         60 
MLGGLLHRGH KIKGTVVLMR KNVLHVNSVT SVGGIIGQGL DLVGSTLDTL TAFLGRPVSL 

        70         80         90        100        110        120 
QLISATKADA NGKGKLGKAT FLEGIITSLP TLGAGQSAFK INFEWDDGSG ILGAFYIKNF 

       130        140        150        160        170        180 
MQTEFFLVSL TLEDIPNHGS IHFVCNSWIY NAKLFKSDRI FFANQTYLPS ETPAPLVKYR 

       190        200        210        220        230        240 
EEELHNLRGD GTGERKEWER VYDYDVYNDL GDPDKGENHA RPVLGGNDTF PYPRRGRTGR 

       250        260        270        280        290        300 
KPTRKDPNSE SRSNDVYLPR DEAFGHLKSS DFLTYGLKSV SQNVLPLLQS AFDLNFTPRE 

       310        320        330        340        350        360 
FDSFDEVHGL YSGGIKLPTD IISKISPLPV LKEIFRTDGE QALKFPPPKV IQVSKSAWMT 

       370        380        390        400        410        420 
DEEFAREMLA GVNPNLIRCL KEFPPRSKLD SQVYGDHTSQ ITKEHLEPNL EGLTVDEAIQ 

       430        440        450        460        470        480 
NKRLFLLGHH DPIMPYLRRI NATSTKAYAT RTILFLKNDG TLRPLAIELS LPHPQGDQSG 

       490        500        510        520        530        540 
AFSQVFLPAD EGVESSIWLL AKAYVVVNDS CYHQLVSHWL NTHAVVEPFI IATNRHLSVV 

       550        560        570        580        590        600 
HPIYKLLHPH YRDTMNINGL ARLSLVNDGG VIEQTFLWGR YSVEMSAVVY KDWVFTDQAL 

       610        620        630        640        650        660 
PADLIKRGMA IEDPSCPHGI RLVIEDYPYA VDGLEIWDAI KTWVHEYVFL YYKSDDTLRE 

       670        680        690        700        710        720 
DPELQACWKE LVEVGHGDKK NEPWWPKMQT REELVEACAI IIWTASALHA AVNFGQYPYG 

       730        740        750        760        770        780 
GLILNRPTLS RRFMPEKGSA EYEELRKNPQ KAYLKTITPK FQTLIDLSVI EILSRHASDE 

       790        800        810        820        830        840 
VYLGERDNPN WTSDTRALEA FKRFGNKLAQ IENKLSERNN DEKLRNRCGP VQMPYTLLLP 

       850 
SSKEGLTFRG IPNSISI 

« Hide

References

[1]"Isolation and characterization of a soybean (Glycine max) lipoxygenase-3 gene."
Yenofsky R.L., Fine M., Liu C.
Mol. Gen. Genet. 211:215-222(1988)
Cited for: NUCLEOTIDE SEQUENCE.
[2]Yenofsky R.L.
Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Position 713 is critical for catalysis but not iron binding in soybean lipoxygenase 3."
Kramer J.A., Johnson K.R., Dunham W.R., Sands R.H., Funk M.O. Jr.
Biochemistry 33:15017-15022(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, MUTAGENESIS OF ASN-713.
Strain: cv. Provar.
[4]"Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme."
Skrzypczak-Jankun E., Amzel L.M., Kroa B.A., Funk M.O. Jr.
Proteins 29:15-31(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Strain: cv. Provar.
[5]"Structural and thermochemical characterization of lipoxygenase-catechol complexes."
Pham C., Jankun J., Skrzypczak-Jankun E., Flowers R.A., Funk M.O. Jr.
Biochemistry 37:17952-17957(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Strain: cv. Provar.
[6]"Three-dimensional structure of a purple lipoxygenase."
Skrzypczak-Jankun E., Bross R.A., Carroll R.T., Dunham W.R., Funk M.O. Jr.
J. Am. Chem. Soc. 123:10814-10820(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON IONS AND SUBSTRATE.
Strain: cv. Provar.
[7]"Structure of curcumin in complex with lipoxygenase and its significance in cancer."
Skrzypczak-Jankun E., Zhou K., McCabe N.P., Selman S.H., Jankun J.
Int. J. Mol. Med. 12:17-24(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH IRON IONS AND CURCUMIN.
[8]"Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead."
Skrzypczak-Jankun E., Zhou K., Jankun J.
Int. J. Mol. Med. 12:415-420(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH IRON IONS AND THE INHIBITOR EPIGALLO-CATECHIN.
[9]"Soybean lipoxygenase-3 in complex with 4-nitrocatechol."
Skrzypczak-Jankun E., Borbulevych O.Y., Jankun J.
Acta Crystallogr. D 60:613-615(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH IRON IONS AND 4-NITROCATECHOL.
[10]"Lipoxygenase interactions with natural flavonoid, quercetin, reveal a complex with protocatechuic acid in its X-ray structure at 2.1 A resolution."
Borbulevych O.Y., Jankun J., Selman S.H., Skrzypczak-Jankun E.
Proteins 54:13-19(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH IRON IONS AND PROTOCATECHUIC ACID.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06928 Genomic DNA. Translation: CAA30016.1.
X13302 mRNA. Translation: CAA31664.1. Sequence problems.
U50081 mRNA. Translation: AAB41272.1.
PIRS01864.
RefSeqNP_001235383.1. NM_001248454.1.
UniGeneGma.30739.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HU9X-ray2.20A1-857[»]
1IK3X-ray2.00A1-857[»]
1JNQX-ray2.10A1-857[»]
1LNHX-ray2.60A1-857[»]
1N8QX-ray2.10A1-857[»]
1NO3X-ray2.15A1-857[»]
1ROVX-ray2.00A1-857[»]
1RRHX-ray2.00A1-857[»]
1RRLX-ray2.09A/B1-857[»]
ProteinModelPortalP09186.
SMRP09186. Positions 7-857.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID547869.
KEGGgmx:547869.

Enzyme and pathway databases

UniPathwayUPA00382.

Gene expression databases

GenevestigatorP09186.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001246. LipOase_pln.
IPR027433. Lipoxygenase_domain_3.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERPTHR11771. PTHR11771. 1 hit.
PfamPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09186.

Entry information

Entry nameLOX3_SOYBN
AccessionPrimary (citable) accession number: P09186
Secondary accession number(s): Q39838
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways