Reviewed,
UniProtKB/Swiss-Prot P29114 (LOX1_HORVU)
Last modified
June 16, 2009.
Version 69.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Lipoxygenase 1 EC=1.13.11.12 | ||||
| Gene names |
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| Organism | Hordeum vulgare (Barley) | ||||
| Taxonomic identifier | 4513 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum |
Protein attributes
| Sequence length | 862 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 | |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis Oxylipin biosynthesis |
| Ligand | Iron Metal-binding |
| Molecular function | Dioxygenase Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxylipin biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW lipoxygenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 862 | 862 | Lipoxygenase 1 | PRO_0000220723 | |||||
Regions | |||||||||
| Domain | 34 – 161 | 128 | PLAT | ||||||
| Domain | 164 – 862 | 699 | Lipoxygenase | ||||||
Sites | |||||||||
| Metal binding | 517 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 522 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 708 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 712 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 862 | 1 | Iron; via carboxylate; catalytic By similarity | ||||||
Sequences
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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. | |
| PIR | S21772. S22236. T05941. |
| UniGene | Hv.9141 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FGT based on UniProtKB P08170. |
| ModBase | Search... |
Organism-specific databases | |
| Gramene | P29114. |
Enzyme and pathway databases | |
| BRENDA | 1.13.11.12. 283. |
Family and domain databases | |
| InterPro | IPR000907. LipOase. IPR013819. LipOase_C. IPR001024. LipOase_LH2. IPR001246. LipOase_pln. [Graphical view] |
| Gene3D | G3DSA:2.60.60.20. Lipase_LipOase. 1 hit. |
| PANTHER | PTHR11771. LipOase. 1 hit. |
| Pfam | PF00305. Lipoxygenase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view] |
| PRINTS | PR00087. LIPOXYGENASE. PR00468. PLTLPOXGNASE. |
| SMART | SM00308. LH2. 1 hit. [Graphical view] |
| PROSITE | PS00711. LIPOXYGENASE_1. 1 hit. PS00081. LIPOXYGENASE_2. 1 hit. PS51393. LIPOXYGENASE_3. 1 hit. PS50095. PLAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LOX1_HORVU | ||||||||
| Accession | Primary (citable) accession number: P29114 Secondary accession number(s): Q42845, Q84QC4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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