P38415 (LOXA_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Linoleate 9S-lipoxygenase A
EC=1.13.11.58

Alternative name(s):
Lipoxygenase A

Gene names

Name:	LOX1.1
Synonyms:	LOXA

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [Reference proteome]

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	860 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate.
Cofactor	Binds 1 iron ion per subunit. Iron is tightly bound By similarity.
Pathway	Lipid metabolism; oxylipin biosynthesis.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in germinating seeds as well as in ripening fruit.
Sequence similarities	Belongs to the lipoxygenase family. Contains 1 lipoxygenase domain. Contains 1 PLAT domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Oxylipin biosynthesis
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	oxylipin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	iron ion binding Inferred from electronic annotation. Source: InterPro lipoxygenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 860	860	Linoleate 9S-lipoxygenase A		PRO_0000220705
Regions
	Domain	29 – 159	131	PLAT
	Domain	162 – 860	699	Lipoxygenase
Sites
	Metal binding	521	1	Iron; catalytic By similarity
	Metal binding	526	1	Iron; catalytic By similarity
	Metal binding	712	1	Iron; catalytic By similarity
	Metal binding	716	1	Iron; catalytic By similarity
	Metal binding	860	1	Iron; via carboxylate; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P38415 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 43D1091853469426	FASTA	860	96,765
	10 20 30 40 50 60 MLGQLVGGLI GGHHDSKKVK GTVVMMKKNA LDFTDLAGSL TDKIFEALGQ KVSFQLISSV 70 80 90 100 110 120 QSDPANGLQG KHSNPAYLEN FLLTLTPLAA GETAFGVTFD WNEEFGVPGA FVIKNMHINE 130 140 150 160 170 180 FFLKSLTLED VPNHGKVHFV CNSWVYPSFR YKSDRIFFAN QPYLPSETPE LLRKYRENEL 190 200 210 220 230 240 VTLRGDGTGK REAWDRIYDY DVYNDLGNPD QGKENVRTTL GGSADYPYPR RGRTGRPPTR 250 260 270 280 290 300 TDPKSESRIP LILSLDIYVP RDERFGHLKM SDFLTYALKS IVQFILPELH ALFDGTPNEF 310 320 330 340 350 360 DSFEDVLRLY EGGIKLPQGP LFKALTDAIP LEMIRELLRT DGEGILRFPT PLVIKDSKTA 370 380 390 400 410 420 WRTDEEFARE MLAGVNPVII SRLEEFPPKS KLDPELYGNQ NSTITAEHIE GKLDGLTIDE 430 440 450 460 470 480 AINSNKLFIL NHHDVLIPYL RRINTTTTKT YASRTLLFLQ DNGSLKPLAI ELSLPHPDGD 490 500 510 520 530 540 QFGVTSKVYT PSDQGVEGSI WQLAKAYVAV NDSGVHQLIS HWLNTHAVIE PFVIATNRQL 550 560 570 580 590 600 SVLHPIHKLL YPHFRDTMNI NALARQILIN AGGVLESTVF PSKFAMEMSA VVYKDWVFPD 610 620 630 640 650 660 QALPADLVKR GVAVEDSSSP HGVRLLIDDY PYAVDGLEIW SAIKSWVTDY CSFYYGSNEE 670 680 690 700 710 720 ILKDNELQAW WKEVREVGHG DKKNEPWWAE METPQELIDS CTTIIWIASA LHAAVNFGQY 730 740 750 760 770 780 PYAGYLPNRP TVSRKFMPEP GTPEYEELKK NPDKAFLKTI TAQLQTLLGV SLIEILSRHT 790 800 810 820 830 840 TDEIYLGQRE SPEWTKDKEP LAAFERFGNK LTDIEKQIMQ RNGNNILTNR TGPVNAPYTL 850 860 LFPTSEGGLT GKGIPNSVSI

References

[1]

"The cloning of two tomato lipoxygenase genes and their differential expression during fruit ripening." Ferrie B.J., Beaudoin N., Burkhart W., Bowsher C.G., Rothstein S.J. Plant Physiol. 106:109-118(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Caruso. Tissue: Pericarp.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U09026 mRNA. Translation: AAA53184.1.
RefSeq	NP_001234856.1. NM_001247927.1.
UniGene	Les.3668.
3D structure databases
ProteinModelPortal	P38415.
SMR	P38415. Positions 18-860.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	Solyc08g014000.2.1; Solyc08g014000.2.1; Solyc08g014000.2.
GeneID	543994.
Enzyme and pathway databases
UniPathway	UPA00382.
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

LOXA_SOLLC

Accession

Primary (citable) accession number: P38415

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program