P27481 (LOXB_PHAVU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Linoleate 9S-lipoxygenase EC=1.13.11.58 Alternative name(s): Lipoxygenase EC=1.13.11.12
Organism	Phaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifier	3885 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Phaseolus

Protein attributes

Sequence length	741 AA.
Sequence status	Fragment.
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. Linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate. Alpha-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate.
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 Fatty acid metabolism Lipid biosynthesis Lipid metabolism 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-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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›741	›741	Linoleate 9S-lipoxygenase		PRO_0000220716
Regions
	Domain	‹1 – 53	›53	PLAT
	Domain	56 – 741	686	Lipoxygenase
Sites
	Metal binding	407	1	Iron; catalytic By similarity
	Metal binding	412	1	Iron; catalytic By similarity
	Metal binding	598	1	Iron; catalytic By similarity
	Metal binding	602	1	Iron; catalytic By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	741	1

Sequences

	Sequence		Length	Mass (Da)
	P27481 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 2F2CDD5979606AC1	FASTA	741	84,197
	10 20 30 40 50 60 IPGAFYIKNF MQVEFYLKSL TLEDIPNHGT IHFICNSWIY NSKVYKSDRI FFANNTYLPS 70 80 90 100 110 120 ETPAPLLKYR EEELKNVRGD GSGERKEWDR VYDYDVYNDL GNPDKGAALA RPVLGGSTLP 130 140 150 160 170 180 YPRRGRTGRP KTKKDPNSEK PSDFVYLPRD EAFGHLKSSD FLAYGLKSVS QDVLPVLTDA 190 200 210 220 230 240 FDGNLLSLEF DNFAEVHKLY EGGVTLPTNF LSKYAPIPIV KEIFRSDGEQ FLKYPPPKVM 250 260 270 280 290 300 QVNKSAWMTD EEFARETIAG VNPNVIKSLE EFPPRSKLDT QSFGDHTSII TKEHLEINLG 310 320 330 340 350 360 GLTVEQAIQS KKLFILDHHD YLIPYLRRIN ASATKTYATR TIFFLKSDGT LAPLAIELSK 370 380 390 400 410 420 PHPQGDEHGP VSEVYVPAYE GVEAYIWLLA KAYVVVNDSC YHQLVSHWLN THAVVEPFVL 430 440 450 460 470 480 ATNRQLSVVH PVYKLLFPHY RDTMNINSLA RKSLVNADGI IEKTFLWGRY ALELSAVIYK 490 500 510 520 530 540 DWSLHDQALP NDLVKRGVAV KDPSAPHGVK LVIEDYPYAS DGLEIWDAIK SWVVEYVAFY 550 560 570 580 590 600 YKSDEVLQQD SELQAWWKEL VQVGHGDLKD KPWWPKMQSR ENLVEVSTTL IWIASALHAA 610 620 630 640 650 660 VNFGQYPYGG LILNRPTISR RFMPEKGSAE YAALAKNPEK EFLKTITGKK ETLIDLTVIE 670 680 690 700 710 720 ILSRHASDEI YLGERDGGDH WTSDAGPLEA FKRFGKKLAE IEKKLVQKNN DETLRNRTGP 730 740 AKMPYTLLYP SSEEGLTFRG I

References

[1]

"Spatial and temporal accumulation of defense gene transcripts in bean (Phaseolus vulgaris) leaves in relation to bacteria-induced hypersensitive cell death." Slusarenko A.J., Meier B.M., Shaw N. Mol. Plant Microbe Interact. 6:453-466(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Red Mexican. Tissue: Leaf.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X63521 mRNA. Translation: CAA45086.1.
PIR	S18906.
3D structure databases
ProteinModelPortal	P27481.
SMR	P27481. Positions 1-741.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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.
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

LOXB_PHAVU

Accession

Primary (citable) accession number: P27481

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	April 3, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program