Reviewed, UniProtKB/Swiss-Prot P93184 (LOX21_HORVU)

Names and origin

Protein names

Recommended name:
    Lipoxygenase 2.1, chloroplastic
    EC=1.13.11.12
Alternative name(s):
    LOX-100
    LOX2:Hv:1

Gene names

Name:

LOX2.1

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	936 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. This enzyme is possibly involved in jasmonic acid synthesis. It exhibits linoleate 13-lipoxygenase and arachidonate 15-lipoxygenase activity.
Catalytic activity	Linoleate + O(2) = (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate.
Cofactor	Binds 1 iron ion per subunit. Iron is tightly bound By similarity.
Pathway	Lipid metabolism; oxylipin biosynthesis.
Subcellular location	Plastid › chloroplast.
Induction	Transient induction by exogenous methyl jasmonate, reaching a maximum 48 hours after treatment. Not induced by endogenous jasmonic acid resulting from sorbitol stress.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the lipoxygenase family. Contains 1 lipoxygenase domain. Contains 1 PLAT domain.
Biophysicochemical properties	pH dependence: Optimum pH is 7.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis Oxylipin biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
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 process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro 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
	Transit peptide	1 – ?		Chloroplast Potential
	Chain	? – 936		Lipoxygenase 2.1, chloroplastic		PRO_0000018323
Regions
	Domain	88 – 217	130	PLAT
	Domain	220 – 936	717	Lipoxygenase
Sites
	Metal binding	587	1	Iron; catalytic By similarity
	Metal binding	592	1	Iron; catalytic By similarity
	Metal binding	777	1	Iron; catalytic By similarity
	Metal binding	781	1	Iron; catalytic By similarity
	Metal binding	936	1	Iron; via carboxylate; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P93184-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 567B8519E0B5D959	FASTA	936	105,864
	10 20 30 40 50 60 MLTATKPLVG GACAAPSSSA RRRTFVVPEA RRKPGNGRRT SVSKVGSTST STTTTTTTTL 70 80 90 100 110 120 SADSNGAAVG TVTRPDVHVQ DRTHATEMKA TVTVHMSKAA GVRDFLYDLI LKTWLHVDLV 130 140 150 160 170 180 SSELDPQTGQ EREPISGAVK HSGRVDDEWD MYEATFKVPA SFGPIGAVQV TNYHHSEMLL 190 200 210 220 230 240 GDIEVFPTGQ EESAVTFHCK SWIDPSHCTP DKRVFFPAHS YLPSQTPKGV EGLRKRELEI 250 260 270 280 290 300 LRGTGCGERK EHDRIYDYDV YNDLGNPDDD NNPTTRPVLG GKEHPYPRRC RTGRPRSKKD 310 320 330 340 350 360 PFSEERSHKE HIYVPRDEAF TERKMGAFDT KKFMSQLHAL TTGLKTAKHK SQSFPSLSAI 370 380 390 400 410 420 DQLYDDNFRN QPVQPEGGKL RFVIDLLETE LLHLFKLEGA AFLEGIRRVF KFETPEIHDR 430 440 450 460 470 480 DKFAWFRDEE FARQTIAGMN PMSIQLVTEF PIKSNLDEAT YGPADSLITK EVVEEQIRRV 490 500 510 520 530 540 MTADEAVQNK KLFMLDYHDL LLPYVHKVRK LDGTTLYGSR ALFFLTADGT LRPIAIELTR 550 560 570 580 590 600 PKSKKKPQWR QVFTPGCDGS VTGSWLWQLA KAHILAHDAG VHQLVSHWLR THACTEPYII 610 620 630 640 650 660 AANRQLSQMH PVYRLLHPHF RFTMEINAQA RAMLINAGGI IEGSFVPGEY SLELSSVAYD 670 680 690 700 710 720 QQWRFDMEAL PEDLIRRGMA VRNPNGELEL AIEDYPYAND GLLVWDAIKQ WALTYVQHYY 730 740 750 760 770 780 PCAADIVDDE ELQAWWTEVR TKGHADKQDE PWWPELDSHE NLAQTLATIM WVTSGHHAAV 790 800 810 820 830 840 NFGQYPMAGY IPNRPTMARR NMPTEIGGDD MRDFVEAPEK VLLDTFPSQY QSAIVLAILD 850 860 870 880 890 900 LLSTHSSDEE YMGTHEEPAW TKDGVINQAF EEFKESTRKI VEQVDEWNND PDRKNRHGAG 910 920 930 MVPYVLLRPS DGDPTDGDPT DEKMVMEMGI PNSISI

References

[1]

"Characterization of a methyljasmonate-inducible lipoxygenase from barley (Hordeum vulgare cv. Salome) leaves." Voeroes K., Feussner I., Kuehn H., Lee J., Graner A., Loebler M., Parthier B., Wasternack C. Eur. J. Biochem. 251:36-44(1998) [PubMed: 9492266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 213-227, CATALYTIC ACTIVITY, FUNCTION, INDUCTION. Strain: cv. Salome. Tissue: Leaf.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U56406 mRNA. Translation: AAC12951.1.
PIR	T06190.
3D structure databases
HSSP	HSSP built from PDB template 2SBL based on UniProtKB P08170.
ModBase	Search...
Organism-specific databases
Gramene	P93184.
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

LOX21_HORVU

Accession

Primary (citable) accession number: P93184

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	May 1, 1997
Last modified:	November 25, 2008
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)