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P08170 (LOX1_SOYBN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. 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 13S-lipoxygenase-1

EC=1.13.11.12
Alternative name(s):
Lipoxygenase-1
Short name=L-1
Gene names
Name:LOX1.1
Synonyms:LOX1
OrganismGlycine max (Soybean) (Glycine hispida) [Reference proteome]
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja

Protein attributes

Sequence length839 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. With linoleate as substrate, L-1 shows a preference for carbon 13 as the site for hydroperoxidation (in contrast to L-2 and L-3, which utilize either carbon 9 or 13). At pH above 8.5, only (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate is produced, but as the pH decreases, the proportion of (9S)-hydroperoxide increases linearly until at pH 6.0 it represents about 25 % of the products. Ref.8

Catalytic activity

Linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate. Ref.5 Ref.8

Alpha-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate. Ref.5 Ref.8

Cofactor

Binds 1 iron ion per subunit. Iron is tightly bound. Ref.7

Pathway

Lipid metabolism; oxylipin biosynthesis.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Induction

The hydroperoxide product serves to activate the resting enzyme. The activation is accompanied by the oxidation of Fe2+entadiene structure. L-1 prefers anionic substrate.

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.

Biophysicochemical properties

pH dependence:

Inactive below pH 6.0. Ref.5 Ref.8

Sequence caution

The sequence CAA47717.1 differs from that shown. Reason: Frameshift at positions 663 and 697.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 839839Seed linoleate 13S-lipoxygenase-1
PRO_0000220717

Regions

Domain16 – 145130PLAT
Domain148 – 839692Lipoxygenase

Sites

Metal binding4991Iron; catalytic Ref.9
Metal binding5041Iron; catalytic Ref.9
Metal binding6901Iron; catalytic Ref.9
Metal binding6941Iron; catalytic
Metal binding8391Iron; via carboxylate; catalytic

Experimental info

Mutagenesis4941H → Q: 37% of wild-type activity. Ref.4 Ref.6
Mutagenesis4941H → S: 8% of wild-type activity. Ref.4 Ref.6
Mutagenesis4951Q → A: Reduces catalytic activity. Ref.4 Ref.6 Ref.11
Mutagenesis4951Q → E: No effect on catalytic activity. Ref.4 Ref.6 Ref.11
Mutagenesis4991H → Q: Inactive. Ref.4 Ref.6
Mutagenesis5041H → Q or S: Inactive. Ref.4 Ref.6
Mutagenesis5171H → Q: 33% of wild-type activity. Ref.4 Ref.6
Mutagenesis5221H → Q: 1% of wild-type activity. Ref.4 Ref.6
Mutagenesis5311H → Q: 20% of wild-type activity. Ref.4 Ref.6
Mutagenesis5421A → G: Changes reaction profile to produce almost equal amounts of 13S- and 9R-hydroperoxyoctadecadienoate. Ref.4 Ref.6 Ref.8
Mutagenesis5421A → S: Little effect on reaction profile. Ref.4 Ref.6 Ref.8
Mutagenesis5421A → T or V: Complete loss of activity. Ref.4 Ref.6 Ref.8
Mutagenesis6901H → Q: Inactive. Ref.4 Ref.6
Mutagenesis6971Q → N or E: Reduces catalytic activity. Ref.4 Ref.6 Ref.11
Sequence conflict426 – 4272AK → RN Ref.3
Sequence conflict558 – 5603LPS → AL Ref.3
Sequence conflict572 – 5743KNW → EL Ref.3
Sequence conflict6411N → P Ref.3
Sequence conflict741 – 7488KLPTLISL → SCRLSLAV Ref.3

Secondary structure

................................................................................................................................................ 839
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08170 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: 1586250ACD3E34A4

FASTA83994,369
        10         20         30         40         50         60 
MFSAGHKIKG TVVLMPKNEL EVNPDGSAVD NLNAFLGRSV SLQLISATKA DAHGKGKVGK 

        70         80         90        100        110        120 
DTFLEGINTS LPTLGAGESA FNIHFEWDGS MGIPGAFYIK NYMQVEFFLK SLTLEAISNQ 

       130        140        150        160        170        180 
GTIRFVCNSW VYNTKLYKSV RIFFANHTYV PSETPAPLVS YREEELKSLR GNGTGERKEY 

       190        200        210        220        230        240 
DRIYDYDVYN DLGNPDKSEK LARPVLGGSS TFPYPRRGRT GRGPTVTDPN TEKQGEVFYV 

       250        260        270        280        290        300 
PRDENLGHLK SKDALEIGTK SLSQIVQPAF ESAFDLKSTP IEFHSFQDVH DLYEGGIKLP 

       310        320        330        340        350        360 
RDVISTIIPL PVIKELYRTD GQHILKFPQP HVVQVSQSAW MTDEEFAREM IAGVNPCVIR 

       370        380        390        400        410        420 
GLEEFPPKSN LDPAIYGDQS SKITADSLDL DGYTMDEALG SRRLFMLDYH DIFMPYVRQI 

       430        440        450        460        470        480 
NQLNSAKTYA TRTILFLRED GTLKPVAIEL SLPHSAGDLS AAVSQVVLPA KEGVESTIWL 

       490        500        510        520        530        540 
LAKAYVIVND SCYHQLMSHW LNTHAAMEPF VIATHRHLSV LHPIYKLLTP HYRNNMNINA 

       550        560        570        580        590        600 
LARQSLINAN GIIETTFLPS KYSVEMSSAV YKNWVFTDQA LPADLIKRGV AIKDPSTPHG 

       610        620        630        640        650        660 
VRLLIEDYPY AADGLEIWAA IKTWVQEYVP LYYARDDDVK NDSELQHWWK EAVEKGHGDL 

       670        680        690        700        710        720 
KDKPWWPKLQ TLEDLVEVCL IIIWIASALH AAVNFGQYPY GGLIMNRPTA SRRLLPEKGT 

       730        740        750        760        770        780 
PEYEEMINNH EKAYLRTITS KLPTLISLSV IEILSTHASD EVYLGQRDNP HWTSDSKALQ 

       790        800        810        820        830 
AFQKFGNKLK EIEEKLVRRN NDPSLQGNRL GPVQLPYTLL YPSSEEGLTF RGIPNSISI 

« Hide

References

[1]"Primary structure of soybean lipoxygenase-1."
Shibata D., Steczko J., Dixon J.E., Hermodson M., Yazdanparast R., Axelrod B.
J. Biol. Chem. 262:10080-10085(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]Fukazawa C., Masayoshi M., Chikafusa F.
Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Bonminori.
Tissue: Cotyledon.
[3]"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] [Europe PMC]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 426-752.
[4]"Conserved histidine residues in soybean lipoxygenase: functional consequences of their replacement."
Steczko J., Donoho G.P., Clemens J.C., Dixon J.E., Axelrod B.
Biochemistry 31:4053-4057(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 479-482, MUTAGENESIS OF SOME HISTIDINE RESIDUES.
[5]"Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-hydroperoxides from linoleic acid by a pH-dependent mechanism."
Gardner H.W.
Biochim. Biophys. Acta 1001:274-281(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SPECIFICITY.
[6]"Identification of the iron-binding histidine residues in soybean lipoxygenase L-1."
Steczko J., Axelrod B.
Biochem. Biophys. Res. Commun. 186:686-689(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SOME HISTIDINE RESIDUES.
[7]"Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1."
Minor W., Steczko J., Bolin J.T., Otwinowski Z., Axelrod B.
Biochemistry 32:6320-6323(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR.
[8]"On the relationships of substrate orientation, hydrogen abstraction, and product stereochemistry in single and double dioxygenations by soybean lipoxygenase-1 and its Ala542Gly mutant."
Coffa G., Imber A.N., Maguire B.C., Laxmikanthan G., Schneider C., Gaffney B.J., Brash A.R.
J. Biol. Chem. 280:38756-38766(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ALA-542, ENZYME KINETICS, REACTION MECHANISM, EPR SPECTROSCOPY.
[9]"The three-dimensional structure of an arachidonic acid 15-lipoxygenase."
Boyington J.C., Gaffney B.J., Amzel L.M.
Science 260:1482-1486(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH IRON IONS.
[10]"Crystal structure of soybean lipoxygenase L-1 at 1.4-A resolution."
Minor W., Steczko J., Stec B., Otwinowski Z., Bolin J.T., Walter R., Axelrod B.
Biochemistry 35:10687-10701(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH IRON IONS.
[11]"Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1."
Tomchick D.R., Phan P., Cymborowski M., Minor W., Holman T.R.
Biochemistry 40:7509-7517(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF WILD-TYPE AND MUTANTS GLN-495 AND GLN-697 IN COMPLEX WITH IRON IONS, MUTAGENESIS OF GLN-495 AND GLN-697.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02795 mRNA. Translation: AAA33986.1.
X67304 mRNA. Translation: CAA47717.1. Frameshift.
PIRDASYL2. S25064.
RefSeqNP_001236153.1. NM_001249224.1.
UniGeneGma.947.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F8NX-ray1.40A1-839[»]
1FGMX-ray1.90A1-839[»]
1FGOX-ray1.62A1-839[»]
1FGQX-ray1.85A1-839[»]
1FGRX-ray1.60A1-839[»]
1FGTX-ray1.62A1-839[»]
1Y4KX-ray1.95A1-839[»]
1YGEX-ray1.40A1-839[»]
2SBLX-ray2.60A/B1-839[»]
3BNBX-ray1.45A1-839[»]
3BNCX-ray1.65A1-839[»]
3BNDX-ray1.60A1-839[»]
3BNEX-ray1.40A1-839[»]
3PZWX-ray1.40A1-839[»]
ProteinModelPortalP08170.
SMRP08170. Positions 1-839.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP08170.
ChEMBLCHEMBL4586.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID547923.
KEGGgmx:547923.

Enzyme and pathway databases

SABIO-RKP08170.
UniPathwayUPA00382.

Gene expression databases

GenevestigatorP08170.

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

EvolutionaryTraceP08170.

Entry information

Entry nameLOX1_SOYBN
AccessionPrimary (citable) accession number: P08170
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 141 of the entry and version 2 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