P27480 (LOXA_PHAVU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Linoleate 9S-lipoxygenase 1
EC=1.13.11.58

Alternative name(s):
Lipoxygenase 1
EC=1.13.11.12

Gene names

Name:	LOXA
Synonyms:	LOX1

Organism

Phaseolus vulgaris (Kidney bean) (French bean)

Taxonomic identifier

3885 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Phaseolus

Protein attributes

Sequence length	862 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. 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.
Subcellular location	Cytoplasm.
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
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	oxylipin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 862	862	Linoleate 9S-lipoxygenase 1		PRO_0000220715
Regions
	Domain	44 – 171	128	PLAT
	Domain	174 – 862	689	Lipoxygenase
Sites
	Metal binding	522	1	Iron; catalytic By similarity
	Metal binding	527	1	Iron; catalytic By similarity
	Metal binding	713	1	Iron; catalytic By similarity
	Metal binding	717	1	Iron; catalytic By similarity
	Metal binding	862	1	Iron; via carboxylate; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27480 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 24D56D1CEE3C191E	FASTA	862	97,155
	10 20 30 40 50 60 MFGILNRGHK IKGTVVLMTK NVFDFNEFVS TTRGGIVGAA GGLFGAATDI VGGIVDGATA 70 80 90 100 110 120 IFSRNIAIQL ISATKTDGLG NGKVGKQTFL EKHLPSLPNL GDRQDAFNVY FEWDENFGIP 130 140 150 160 170 180 EAFYIKNFMQ SEFFLVSLTL EDIPNHGTIH FVCNSWVYNA KSYKRDRIFF ANKTYLPNET 190 200 210 220 230 240 PASLVKYRKE ELENLRGDGT GERKEYDRIY DYAVYNDLGN PDKNKNLART TLGGSSDFPY 250 260 270 280 290 300 PRRGRTGRKS TRKDPKCEIP TSDTYIPRDE NFGHLKSGDF LTYAIKSLTQ NVLPTFQKAF 310 320 330 340 350 360 GFNNEFDTFE DVRGLFEGGL YLPTDVISKI SPIPVLKEIL RTDGEQVLKF PPPHVIRVTK 370 380 390 400 410 420 SAWMTDEEFG REMLAGVNPC LIQRLQEFPP KSKLDVTVYG DQTSTMTKEH LEINLGGLTV 430 440 450 460 470 480 EEALHGNRLF ILDHHDAFIP YLERINDLPT AKCYATRTIL FLKDDNTLKP LAIELSLPNP 490 500 510 520 530 540 GGKGANSRVI LPADGGAEST IWLLAKAYVV VNDSCYHQLM SHWLNTHAVM EPFVIATNRH 550 560 570 580 590 600 LSVLHPIYKL LLPHYRDTMN INALARQSLI NAGGVIERSF LPGEFAVEMS SAVYKSWVFT 610 620 630 640 650 660 DQALPADLIK RGMAVEDPSS PYGLRLVVED YPYAVDGLEI WDTIQTWVKD YVSLYYPTND 670 680 690 700 710 720 AVKKDTELQA WWKEAVEKGH GDLKDKPWWP KLNTPQDLIH TCSIIIWIAS ALHAAVNFGQ 730 740 750 760 770 780 YPYGGFILNR PTITRRLLPE PGTKEYGELT SNYQKAYLRT ITGKVEAIVD LSVIEILSRH 790 800 810 820 830 840 ASDEVYLGQR DNPNWTNNIK ALQAFKRFGQ KLKEIEEKIM GRNKDSSLRN RNGPVKMPYT 850 860 VLLPTCEDEG LTFRGIPNSI SI

References

[1]	"Complex spatial and temporal expression of lipoxygenase genes during Phaseolus vulgaris (L.) development." Eiben H.G., Slusarenko A.J. Plant J. 5:123-135(1994) [PubMed: 8130796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Red Mexican. Tissue: Leaf.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X63525 Genomic DNA. Translation: CAA45088.1.
PIR	S22153.
3D structure databases
ProteinModelPortal	P27480.
SMR	P27480. Positions 8-862.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR008976. Lipase_LipOase. IPR000907. LipOase. IPR013819. LipOase_C. IPR020834. LipOase_CS. IPR020833. LipOase_Fe_BS. 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]
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_PHAVU

Accession

Primary (citable) accession number: P27480

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	September 21, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program