Q9LUW0 (LOX5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Linoleate 9S-lipoxygenase 5, chloroplastic
EC=1.13.11.58

Alternative name(s):
Lipoxygenase 5
Short name=AtLOX5

Gene names

Name:	LOX5
Ordered Locus Names:	At3g22400
ORF Names:	MCB17.13

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	886 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	9S-lipoxygenase that can use linoleic acid or linolenic acid as substrates. Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Function as regulators of root development by controlling the emergence of lateral roots. Ref.5 Ref.6
Catalytic activity	Linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate.
Cofactor	Binds 1 iron ion per subunit By similarity.
Pathway	Lipid metabolism; oxylipin biosynthesis.
Subcellular location	Plastid › chloroplast Ref.4.
Tissue specificity	Expressed in roots. Ref.5
Developmental stage	First observed in lateral root primordia (LRP), from the first pericycle divisions. Disappears before root emergence. Ref.5
Disruption phenotype	Increment in the number of lateral roots, and moderate increase in the length of the primary root. Ref.5
Sequence similarities	Belongs to the lipoxygenase family. Contains 1 lipoxygenase domain. Contains 1 PLAT domain.
Sequence caution	The sequence BAB01777.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Oxylipin biosynthesis
Cellular component	Chloroplast Plastid
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lateral root formation Inferred from mutant phenotype Ref.5. Source: UniProtKB lipid oxidation Inferred from direct assay PubMed 21372125. Source: TAIR negative regulation of defense response to insect Inferred from mutant phenotype PubMed 22474183. Source: TAIR oxylipin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	chloroplast Inferred from direct assay Ref.4. Source: TAIR
Molecular_function	iron ion binding Inferred from electronic annotation. Source: InterPro lipoxygenase activity Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 886	886	Linoleate 9S-lipoxygenase 5, chloroplastic		PRO_0000380594
Regions
	Domain	35 – 180	146	PLAT
	Domain	183 – 886	704	Lipoxygenase
Sites
	Metal binding	542	1	Iron; catalytic By similarity
	Metal binding	547	1	Iron; catalytic By similarity
	Metal binding	733	1	Iron; catalytic By similarity
	Metal binding	737	1	Iron; catalytic By similarity
	Metal binding	886	1	Iron; via carboxylate; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9LUW0 [UniParc]. Last modified July 28, 2009. Version 2. Checksum: 0FF118853811E202	FASTA	886	101,060
	10 20 30 40 50 60 MIHTDIAEIL CVKPKTTKKT KTMEEDVKKT TTMKIEGEVV VMKKNLLDFK DVMASLLDRV 70 80 90 100 110 120 NELLGRRVSL HLISSHQPDP ANEKRGRLGK AAHLEKWVTK IKTSVTAEET AFGVTFDWDE 130 140 150 160 170 180 SMGPPAAFVI KNHHHSQFYL KSLTLRGFPD GEGGATAIHF ICNSWIYPNH RYRSDRVFFS 190 200 210 220 230 240 NKAYLPSETP ELIKELREEE LKNLRGNEKG GEFKEWDRVY DYAYYNDLGA PDKGPDSVRP 250 260 270 280 290 300 VLGGSPELPY PRRGKTGRKS TKSDPKSESR LALLNLNIYV PRDERFSHVK FSDFLAYALK 310 320 330 340 350 360 SVTQVLVPEI ASVCDKTINE FDSFEDVFHL YDGSIKLANG HTISKLRDVI PWEMFRELVR 370 380 390 400 410 420 NDGERFLKYP LPDILKESRS AWRTDEEFAR EMLAGLNPVV ISRLQEFPPK SCLDSAKYGN 430 440 450 460 470 480 QHSSIRTEHI ESNMNGLNVQ EALEQNKLYI LDHHDALMPY LTRINSTNTK TYATRTLLLL 490 500 510 520 530 540 QADGTLKPLA IELSLPHAQG ESYGSVSKVF TPAEKGVEGS VWQLAKAYAA VNDSGYHQLI 550 560 570 580 590 600 SHWLQTHAVI EPFIIASNRQ LSVVHPIHKL LHPHFRDTMN INALARHVLI NSDGVLERTV 610 620 630 640 650 660 FPSRYAMEMS SSIYKNWVFT EQALPKDLLK RGVAVEDPNS DNGVKLLIED YPFAVDGLEI 670 680 690 700 710 720 WSAIKTWVTE YCTFYYNNDK TVQTDTEIQS WWTELRTKGH GDKRHESWWP SMQTRDDLIE 730 740 750 760 770 780 TCTIIIWIAS ALHAAVNFGQ YPYAGFLPNR PTVSRRFMPE PGTDEYAELE EDADVAFLKT 790 800 810 820 830 840 ITPQLQTLLG ISIIEILSMH STDEIYLGQR DSPNWTADDE PLEAFKRFGK ELELIENNII 850 860 870 880 RRNNDKRFKN RTGPVNIPYT LLYPNTTDYT REGGITGKGI PNSVSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S. DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"AtLOX5, the second 9-LOX of Arabidopsis." Kunze S., Fritsche K., Feussner I. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-886.
[4]	"The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions." Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S. Curr. Biol. 14:354-362(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]	"Oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade." Vellosillo T., Martinez M., Lopez M.A., Vicente J., Cascon T., Dolan L., Hamberg M., Castresana C. Plant Cell 19:831-846(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[6]	"Diversity of the enzymatic activity in the lipoxygenase gene family of Arabidopsis thaliana." Bannenberg G., Martinez M., Hamberg M., Castresana C. Lipids 44:85-95(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB022215 Genomic DNA. Translation: BAB01777.1. Sequence problems. CP002686 Genomic DNA. Translation: AEE76630.1. AJ302043 mRNA. Translation: CAC19365.1.
IPI	IPI00543707.
RefSeq	NP_188879.2. NM_113137.3.
UniGene	At.37889.
3D structure databases
HSSP	HSSP built from PDB template 2SBL based on UniProtKB P08170.
ProteinModelPortal	Q9LUW0.
SMR	Q9LUW0. Positions 34-886.
ModBase	Search...
Proteomic databases
PaxDb	Q9LUW0.
PRIDE	Q9LUW0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G22400.1; AT3G22400.1; AT3G22400.
GeneID	821808.
KEGG	ath:AT3G22400.
Organism-specific databases
TAIR	At3g22400.
Phylogenomic databases
eggNOG	NOG69653.
HOGENOM	HOG000230469.
InParanoid	Q9LUW0.
KO	K15718.
OMA	QTIIGIS.
PhylomeDB	Q9LUW0.
ProtClustDB	PLN02337.
Enzyme and pathway databases
UniPathway	UPA00382.
Gene expression databases
Genevestigator	Q9LUW0.
Family and domain databases
Gene3D	2.60.60.20. 1 hit.
InterPro	IPR008976. Lipase_LipOase. IPR000907. LipOase. IPR013819. LipOase_C. IPR020834. LipOase_CS. IPR020833. LipOase_Fe_BS. IPR001024. LipOase_LH2. IPR001246. LipOase_pln. [Graphical view]
PANTHER	PTHR11771. PTHR11771. 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]
SUPFAM	SSF49723. Lipase_LipOase. 1 hit. SSF48484. Lipoxygenase. 1 hit.
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

LOX5_ARATH

Accession

Primary (citable) accession number: Q9LUW0
Secondary accession number(s): Q9FNX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	July 28, 2009
Last modified:	May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program