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Reviewed, UniProtKB/Swiss-Prot P29114 (LOX1_HORVU)

Last modified June 16, 2009. Version 69. 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:
    Lipoxygenase 1
    EC=1.13.11.12
Gene names
Name: LOX1.1
Synonyms: LOXA
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length862 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 = (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.

Developmental stage

In both quiescent and germinating seeds.

Miscellaneous

With linoleate as substrate, lipoxygenase 1 shows a specificity for carbon 9 as the site for hydroperoxidation (in contrast to lipoxygenase 2, which shows a preference for carbon 13).

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 862862Lipoxygenase 1
PRO_0000220723

Regions

Domain34 – 161128PLAT
Domain164 – 862699Lipoxygenase

Sites

Metal binding5171Iron; catalytic By similarity
Metal binding5221Iron; catalytic By similarity
Metal binding7081Iron; catalytic By similarity
Metal binding7121Iron; catalytic By similarity
Metal binding8621Iron; via carboxylate; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
P29114-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: F55954473467BEAA

FASTA86296,393
        10         20         30         40         50         60 
MLLGGLIDTL TGANKSARLK GTVVLMRKNV LDLNDFGATI IDGIGEFLGK GVTCQLISST 

        70         80         90        100        110        120 
AVDQDNGGRG KVGAEAELEQ WVTSLPSLTT GESKFGLTFD WEVEKLGVPG AIVVNNYHSS 

       130        140        150        160        170        180 
EFLLKTITLH DVPGRSGNLT FVANSWIYPA ANYRYSRVFF ANDTYLPSQM PAALKPYRDD 

       190        200        210        220        230        240 
ELRNLRGDDQ QGPYQEHDRI YRYDVYNDLG EGRPILGGNS DHPYPRRGRT ERKPNASDPS 

       250        260        270        280        290        300 
LESRLSLLEQ IYVPRDEKFG HLKTSDFLGY SIKAITQGIL PAVRTYVDTT PGEFDSFQDI 

       310        320        330        340        350        360 
INLYEGGIKL PKVAALEELR KQFPLQLIKD LLPVGGDSLL KLPVPHIIQE NKQAWRTDEE 

       370        380        390        400        410        420 
FAREVLAGVN PVMITRLTEF PPKSSLDPSK FGDHTSTITA EHIEKNLEGL TVQQALESNR 

       430        440        450        460        470        480 
LYILDHHDRF MPFLIDVNNL PGNFIYATRT LFFLRGDGRL TPLAIELSEP IIQGGLTTAK 

       490        500        510        520        530        540 
SKVYTPVPSG SVEGWVWELA KAYVAVNDSG WHQLVSHWLN THAVMEPFVI STNRHLSVTH 

       550        560        570        580        590        600 
PVHKLLSPHY RDTMTINALA RQTLINAGGI FEMTVFPGKF ALGMSAVVYK DWKFTEQGLP 

       610        620        630        640        650        660 
DDLIKRGMAV EDPSSPYKVR LLVSDYPYAA DGLAIWHAIE QYVSEYLAIY YPNDGVLQGD 

       670        680        690        700        710        720 
TEVQAWWKET REVGHGDLKD APWWPKMQSV PELAKACTTI IWIGSALHAA VNFGQYPYAG 

       730        740        750        760        770        780 
FLPNRPTVSR RRMPEPGTEE YAELERDPER AFIHTITSQI QTIIGVSLLE VLSKHSSDEL 

       790        800        810        820        830        840 
YLGQRDTPEW TSDPKALEVF KRFSDRLVEI ESKVVGMNHD PELKNRNGPA KFPYMLLYPN 

       850        860 
TSDHKGAAAG LTAKGIPNSI SI 

« Hide

References

[1]"Primary structure of a lipoxygenase from barley grain as deduced from its cDNA sequence."
van Mechelen J.R., Smits M., Douma A.C., Rouster J., Cameron-Mills V., Heidekamp F., Valk B.E.
Biochim. Biophys. Acta 1254:221-225(1995) [PubMed: 7827128] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Triumph.
[2]"Differential defense reactions in leaf tissues of barley in response to infection by Rhynchosporium secalis and to treatment with a fungal avirulence gene product."
Steiner-Lange S., Fischer A., Boettcher A., Rouhara I., Liedgens H., Schmelzer E., Knogge W.
Mol. Plant Microbe Interact. 16:893-902(2003) [PubMed: 14558691] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 512-862.
[3]"Purification and characterization of two lipoxygenase isoenzymes from germinating barley."
Doderer A., Kokkelink I., van der Veen S., Valk B.E., Schram A.W., Douma A.C.
Biochim. Biophys. Acta 1120:97-104(1992) [PubMed: 1554746] [Abstract]
Cited for: PROTEIN SEQUENCE OF 274-294 AND 832-845.
Strain: cv. Triumph.
Tissue: Embryo.

Cross-references

Sequence databases

L35931 Genomic DNA. Translation: AAA64893.1.
AY220737 mRNA. Translation: AAP04432.1. Different initiation.
PIRS21772.
S22236.
T05941.
UniGeneHv.9141

3D structure databases

HSSPHSSP built from PDB template 1FGT based on UniProtKB P08170.
ModBaseSearch...

Organism-specific databases

GrameneP29114.

Enzyme and pathway databases

BRENDA1.13.11.12. 283.

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...

Entry information

Entry nameLOX1_HORVU
AccessionPrimary (citable) accession number: P29114
Secondary accession number(s): Q42845, Q84QC4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 69 of the entry and version 2 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