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O24370

- LOX21_SOLTU

UniProt

O24370 - LOX21_SOLTU

Protein

Linoleate 13S-lipoxygenase 2-1, chloroplastic

Gene

LOX2.1

Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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

    Binds 1 iron ion per subunit.PROSITE-ProRule annotation

    pH dependencei

    Optimum pH is 7.0.1 Publication

    Pathwayi

    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

    1. iron ion binding Source: InterPro
    2. linoleate 13S-lipoxygenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. oxylipin biosynthetic process Source: UniProtKB-UniPathway

    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: Unplaced

    Subcellular locationi

    Plastidchloroplast stroma. Plastidchloroplast thylakoid
    Note: Associated with the non-appressed part of the thylakoid membrane.

    GO - Cellular componenti

    1. chloroplast stroma Source: UniProtKB-SubCell
    2. chloroplast thylakoid Source: UniProtKB-SubCell

    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

    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

    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_pln.
    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

    MLKPQLQQSS QSTKALIPSW NTNPLFLASF PINILNKNFR LKKKNNFRVH    50
    HNYNGASTTK AVLSSTEKAT GVKAVVTVQK QVNLNLSRGL DDIGDLLGKS 100
    LLLWIVAAEL DHKTGIEKPG IRAYAHRGRD VDGDTHYEAD FVIPQDFGEV 150
    GAILIENEHH KEMYVKNIVI DGFVHGKVEI TCNSWVHSKF DNPDKRIFFT 200
    NKSYLPSQTP SGVSRLREEE LVTLRGDGIG ERKVFERIYD YDVYNDLGEA 250
    DSNNDDAKRP VLGGKELPYP RRCKTGRPRS KKDPLSETRS TFVYVPRDEA 300
    FSEVKSVAFS GNTVYSVLHA VVPALESVVT DPNLGFPHFP AIDSLFNVGV 350
    DLPGLGDKKS GLFNVVPRLI KAISDTRKDV LLFESPQLVQ RDKFSWFRDV 400
    EFARQTLAGL NPYSIRLVTE WPLRSKLDPK VYGPPESEIT KELIEKEIGN 450
    YMTVEQAVQQ KKLFILDYHD LLLPYVNKVN ELKGSMLYGS RTIFFLTPQG 500
    TLKPLAIELT RPPVDDKPQW KEVYSPNDWN ATGAWLWKLA KAHVLSHDSG 550
    YHQLVSHWLR THCCTEPYII ASNRQLSAMH PIYRLLHPHF RYTMEINALA 600
    REALINANGV IESSFFPGKY AIELSSIAYG AEWRFDQEAL PQNLISRGLA 650
    VEDPNEPHGL KLAIEDYPFA NDGLVLWDIL KQWVTNYVNH YYPQTNLIES 700
    DKELQAWWSE IKNVGHGDKR DEPWWPELKT PNDLIGIITT IVWVTSGHHA 750
    AVNFGQYSYA GYFPNRPTVA RSKMPTEDPT AEEWEWFMNK PEEALLRCFP 800
    SQIQATKVMA ILDVLSNHSP DEEYIGEKIE PYWAEDPVIN AAFEVFSGKL 850
    KELEGIIDAR NNDSKLSNRN GAGVMPYELL KPYSEPGVTG KGVPYSISI 899
    Length:899
    Mass (Da):101,937
    Last modified:January 1, 1998 - v1
    Checksum:i43E9D512C0E808FF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X96405 mRNA. Translation: CAA65268.1 .
    PIRi T07062.
    RefSeqi NP_001274843.1. NM_001287914.1.
    UniGenei Stu.18313.

    3D structure databases

    ProteinModelPortali O24370.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 102596122.
    KEGGi sot:102596122.

    Phylogenomic databases

    KOi K00454.

    Enzyme and pathway databases

    UniPathwayi UPA00382 .

    Family and domain databases

    Gene3Di 2.60.60.20. 1 hit.
    4.10.372.10. 1 hit.
    InterProi IPR008976. Lipase_LipOase.
    IPR000907. LipOase.
    IPR013819. LipOase_C.
    IPR020834. LipOase_CS.
    IPR020833. LipOase_Fe_BS.
    IPR001246. LipOase_pln.
    IPR027433. Lipoxygenase_domain_3.
    IPR001024. PLAT/LH2_dom.
    [Graphical view ]
    PANTHERi PTHR11771. PTHR11771. 1 hit.
    Pfami PF00305. Lipoxygenase. 1 hit.
    PF01477. PLAT. 1 hit.
    [Graphical view ]
    PRINTSi PR00087. LIPOXYGENASE.
    PR00468. PLTLPOXGNASE.
    SMARTi SM00308. LH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48484. SSF48484. 1 hit.
    SSF49723. SSF49723. 1 hit.
    PROSITEi PS00711. LIPOXYGENASE_1. 1 hit.
    PS00081. LIPOXYGENASE_2. 1 hit.
    PS51393. LIPOXYGENASE_3. 1 hit.
    PS50095. PLAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 93 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