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Protein

Linoleate 13S-lipoxygenase 2-1, chloroplastic

Gene

LOX2.1

Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plant lipoxygenase involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence. May not be involved in the bulk production of jasmonate upon wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred substrate, before linoleic and arachidonic acids. Has also some activity with phosphatidylglycerol, but not with galactolipids.2 Publications

Catalytic activityi

Linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate.
Alpha-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate.

Cofactori

Fe cationPROSITE-ProRule annotationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation

pH dependencei

Optimum pH is 7.0.1 Publication

Pathway: oxylipin biosynthesis

This protein is involved in the pathway oxylipin biosynthesis, which is part of Lipid metabolism.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway oxylipin biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi557 – 5571Iron; catalyticPROSITE-ProRule annotation
Metal bindingi562 – 5621Iron; catalyticPROSITE-ProRule annotation
Metal bindingi749 – 7491Iron; catalyticPROSITE-ProRule annotation
Metal bindingi753 – 7531Iron; catalyticPROSITE-ProRule annotation
Metal bindingi899 – 8991Iron; via carboxylate; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  • linoleate 13S-lipoxygenase activity Source: CACAO
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Oxylipin biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00382.

Names & Taxonomyi

Protein namesi
Recommended name:
Linoleate 13S-lipoxygenase 2-1, chloroplastic (EC:1.13.11.12)
Alternative name(s):
Lipoxygenase 2-1
Gene namesi
Name:LOX2.1
Synonyms:LOX-H1
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040ChloroplastSequence AnalysisAdd
BLAST
Chaini41 – 899859Linoleate 13S-lipoxygenase 2-1, chloroplasticPRO_0000412927Add
BLAST

Expressioni

Tissue specificityi

Expressed in leaves and floral buds.1 Publication

Inductioni

Up-regulated by jasmonate and abscisic acid treatment. Up-regulated localy and systemically at the transcript levels 6 hours after wounding, but the protein levels remain constant. Not induced by pathogen infection.3 Publications

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi4113.PGSC0003DMT400081909.

Structurei

3D structure databases

ProteinModelPortaliO24370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 200123PLATPROSITE-ProRule annotationAdd
BLAST
Domaini203 – 899697LipoxygenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the lipoxygenase family.Curated
Contains 1 lipoxygenase domain.PROSITE-ProRule annotation
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiO24370.
KOiK00454.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001246. LipOase_plant.
IPR027433. Lipoxygenase_domain_3.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O24370-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKPQLQQSS QSTKALIPSW NTNPLFLASF PINILNKNFR LKKKNNFRVH
60 70 80 90 100
HNYNGASTTK AVLSSTEKAT GVKAVVTVQK QVNLNLSRGL DDIGDLLGKS
110 120 130 140 150
LLLWIVAAEL DHKTGIEKPG IRAYAHRGRD VDGDTHYEAD FVIPQDFGEV
160 170 180 190 200
GAILIENEHH KEMYVKNIVI DGFVHGKVEI TCNSWVHSKF DNPDKRIFFT
210 220 230 240 250
NKSYLPSQTP SGVSRLREEE LVTLRGDGIG ERKVFERIYD YDVYNDLGEA
260 270 280 290 300
DSNNDDAKRP VLGGKELPYP RRCKTGRPRS KKDPLSETRS TFVYVPRDEA
310 320 330 340 350
FSEVKSVAFS GNTVYSVLHA VVPALESVVT DPNLGFPHFP AIDSLFNVGV
360 370 380 390 400
DLPGLGDKKS GLFNVVPRLI KAISDTRKDV LLFESPQLVQ RDKFSWFRDV
410 420 430 440 450
EFARQTLAGL NPYSIRLVTE WPLRSKLDPK VYGPPESEIT KELIEKEIGN
460 470 480 490 500
YMTVEQAVQQ KKLFILDYHD LLLPYVNKVN ELKGSMLYGS RTIFFLTPQG
510 520 530 540 550
TLKPLAIELT RPPVDDKPQW KEVYSPNDWN ATGAWLWKLA KAHVLSHDSG
560 570 580 590 600
YHQLVSHWLR THCCTEPYII ASNRQLSAMH PIYRLLHPHF RYTMEINALA
610 620 630 640 650
REALINANGV IESSFFPGKY AIELSSIAYG AEWRFDQEAL PQNLISRGLA
660 670 680 690 700
VEDPNEPHGL KLAIEDYPFA NDGLVLWDIL KQWVTNYVNH YYPQTNLIES
710 720 730 740 750
DKELQAWWSE IKNVGHGDKR DEPWWPELKT PNDLIGIITT IVWVTSGHHA
760 770 780 790 800
AVNFGQYSYA GYFPNRPTVA RSKMPTEDPT AEEWEWFMNK PEEALLRCFP
810 820 830 840 850
SQIQATKVMA ILDVLSNHSP DEEYIGEKIE PYWAEDPVIN AAFEVFSGKL
860 870 880 890
KELEGIIDAR NNDSKLSNRN GAGVMPYELL KPYSEPGVTG KGVPYSISI
Length:899
Mass (Da):101,937
Last modified:January 1, 1998 - v1
Checksum:i43E9D512C0E808FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96405 mRNA. Translation: CAA65268.1.
PIRiT07062.
RefSeqiNP_001274843.1. NM_001287914.1.
UniGeneiStu.18313.

Genome annotation databases

GeneIDi102596122.
KEGGisot:102596122.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96405 mRNA. Translation: CAA65268.1.
PIRiT07062.
RefSeqiNP_001274843.1. NM_001287914.1.
UniGeneiStu.18313.

3D structure databases

ProteinModelPortaliO24370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4113.PGSC0003DMT400081909.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102596122.
KEGGisot:102596122.

Phylogenomic databases

InParanoidiO24370.
KOiK00454.

Enzyme and pathway databases

UniPathwayiUPA00382.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001246. LipOase_plant.
IPR027433. Lipoxygenase_domain_3.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns."
    Royo J., Vancanneyt G., Perez A.G., Sanz C., Stormann K., Rosahl S., Sanchez-Serrano J.J.
    J. Biol. Chem. 271:21012-21019(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY WOUNDING; JASMONATE AND ABSCISIC ACID, BIOPHYSICOCHEMICAL PROPERTIES.
  2. "A leaf lipoxygenase of potato induced specifically by pathogen infection."
    Kolomiets M.V., Chen H., Gladon R.J., Braun E.J., Hannapel D.J.
    Plant Physiol. 124:1121-1130(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY PATHOGEN.
  3. "Lipoxygenase H1 gene silencing reveals a specific role in supplying fatty acid hydroperoxides for aliphatic aldehyde production."
    Leon J., Royo J., Vancanneyt G., Sanz C., Silkowski H., Griffiths G., Sanchez-Serrano J.J.
    J. Biol. Chem. 277:416-423(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
  4. "Differential distribution of the lipoxygenase pathway enzymes within potato chloroplasts."
    Farmaki T., Sanmartin M., Jimenez P., Paneque M., Sanz C., Vancanneyt G., Leon J., Sanchez-Serrano J.J.
    J. Exp. Bot. 58:555-568(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION BY WOUNDING.

Entry informationi

Entry nameiLOX21_SOLTU
AccessioniPrimary (citable) accession number: O24370
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 1, 1998
Last modified: June 24, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

99% depletion of LOX-H1 by co-suppression-mediated gene silencing has no effect on the basal or wound-induced levels of jasmonates but results in a marked reduction in the production of volatile aliphatic C6 aldehydes.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.