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P93184 (LOX21_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Lipoxygenase 2.1, chloroplastic

EC=1.13.11.12
Alternative name(s):
LOX-100
LOX2:Hv:1
Gene names
Name:LOX2.1
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length936 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. This enzyme is possibly involved in jasmonic acid synthesis. It exhibits linoleate 13-lipoxygenase and arachidonate 15-lipoxygenase activity. Ref.1

Catalytic activity

Linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate. Ref.1

Alpha-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate. Ref.1

Cofactor

Binds 1 iron ion per subunit. Iron is tightly bound By similarity.

Pathway

Lipid metabolism; oxylipin biosynthesis.

Subcellular location

Plastidchloroplast.

Induction

Transient induction by exogenous methyl jasmonate, reaching a maximum 48 hours after treatment. Not induced by endogenous jasmonic acid resulting from sorbitol stress. Ref.1

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Oxylipin biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processoxylipin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

linoleate 13S-lipoxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast Potential
Chain? – 936Lipoxygenase 2.1, chloroplasticPRO_0000018323

Regions

Domain88 – 217130PLAT
Domain220 – 936717Lipoxygenase

Sites

Metal binding5871Iron; catalytic By similarity
Metal binding5921Iron; catalytic By similarity
Metal binding7771Iron; catalytic By similarity
Metal binding7811Iron; catalytic By similarity
Metal binding9361Iron; via carboxylate; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
P93184 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 567B8519E0B5D959

FASTA936105,864
        10         20         30         40         50         60 
MLTATKPLVG GACAAPSSSA RRRTFVVPEA RRKPGNGRRT SVSKVGSTST STTTTTTTTL 

        70         80         90        100        110        120 
SADSNGAAVG TVTRPDVHVQ DRTHATEMKA TVTVHMSKAA GVRDFLYDLI LKTWLHVDLV 

       130        140        150        160        170        180 
SSELDPQTGQ EREPISGAVK HSGRVDDEWD MYEATFKVPA SFGPIGAVQV TNYHHSEMLL 

       190        200        210        220        230        240 
GDIEVFPTGQ EESAVTFHCK SWIDPSHCTP DKRVFFPAHS YLPSQTPKGV EGLRKRELEI 

       250        260        270        280        290        300 
LRGTGCGERK EHDRIYDYDV YNDLGNPDDD NNPTTRPVLG GKEHPYPRRC RTGRPRSKKD 

       310        320        330        340        350        360 
PFSEERSHKE HIYVPRDEAF TERKMGAFDT KKFMSQLHAL TTGLKTAKHK SQSFPSLSAI 

       370        380        390        400        410        420 
DQLYDDNFRN QPVQPEGGKL RFVIDLLETE LLHLFKLEGA AFLEGIRRVF KFETPEIHDR 

       430        440        450        460        470        480 
DKFAWFRDEE FARQTIAGMN PMSIQLVTEF PIKSNLDEAT YGPADSLITK EVVEEQIRRV 

       490        500        510        520        530        540 
MTADEAVQNK KLFMLDYHDL LLPYVHKVRK LDGTTLYGSR ALFFLTADGT LRPIAIELTR 

       550        560        570        580        590        600 
PKSKKKPQWR QVFTPGCDGS VTGSWLWQLA KAHILAHDAG VHQLVSHWLR THACTEPYII 

       610        620        630        640        650        660 
AANRQLSQMH PVYRLLHPHF RFTMEINAQA RAMLINAGGI IEGSFVPGEY SLELSSVAYD 

       670        680        690        700        710        720 
QQWRFDMEAL PEDLIRRGMA VRNPNGELEL AIEDYPYAND GLLVWDAIKQ WALTYVQHYY 

       730        740        750        760        770        780 
PCAADIVDDE ELQAWWTEVR TKGHADKQDE PWWPELDSHE NLAQTLATIM WVTSGHHAAV 

       790        800        810        820        830        840 
NFGQYPMAGY IPNRPTMARR NMPTEIGGDD MRDFVEAPEK VLLDTFPSQY QSAIVLAILD 

       850        860        870        880        890        900 
LLSTHSSDEE YMGTHEEPAW TKDGVINQAF EEFKESTRKI VEQVDEWNND PDRKNRHGAG 

       910        920        930 
MVPYVLLRPS DGDPTDGDPT DEKMVMEMGI PNSISI 

« Hide

References

[1]"Characterization of a methyljasmonate-inducible lipoxygenase from barley (Hordeum vulgare cv. Salome) leaves."
Voeroes K., Feussner I., Kuehn H., Lee J., Graner A., Loebler M., Parthier B., Wasternack C.
Eur. J. Biochem. 251:36-44(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 213-227, CATALYTIC ACTIVITY, FUNCTION, INDUCTION.
Strain: cv. Salome.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U56406 mRNA. Translation: AAC12951.1.
PIRT06190.

3D structure databases

ProteinModelPortalP93184.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP93184.

Enzyme and pathway databases

UniPathwayUPA00382.

Gene expression databases

GenevestigatorP93184.

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...

Entry information

Entry nameLOX21_HORVU
AccessionPrimary (citable) accession number: P93184
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: May 1, 1997
Last modified: October 16, 2013
This is version 84 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

PATHWAY comments

Index of metabolic and biosynthesis pathways