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P08170

- LOX1_SOYBN

UniProt

P08170 - LOX1_SOYBN

Protein

Seed linoleate 13S-lipoxygenase-1

Gene

LOX1.1

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    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. With linoleate as substrate, L-1 shows a preference for carbon 13 as the site for hydroperoxidation (in contrast to L-2 and L-3, which utilize either carbon 9 or 13). At pH above 8.5, only (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate is produced, but as the pH decreases, the proportion of (9S)-hydroperoxide increases linearly until at pH 6.0 it represents about 25 % of the products.1 Publication

    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. Iron is tightly bound.1 PublicationPROSITE-ProRule annotation

    pH dependencei

    Inactive below pH 6.0.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi499 – 4991Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi504 – 5041Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi690 – 6901Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi694 – 6941Iron; catalytic
    Metal bindingi839 – 8391Iron; via carboxylate; catalytic

    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

    SABIO-RKP08170.
    UniPathwayiUPA00382.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Seed linoleate 13S-lipoxygenase-1 (EC:1.13.11.12)
    Alternative name(s):
    Lipoxygenase-1
    Short name:
    L-1
    Gene namesi
    Name:LOX1.1
    Synonyms:LOX1
    OrganismiGlycine max (Soybean) (Glycine hispida)
    Taxonomic identifieri3847 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
    ProteomesiUP000008827: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi494 – 4941H → Q: 37% of wild-type activity.
    Mutagenesisi494 – 4941H → S: 8% of wild-type activity.
    Mutagenesisi495 – 4951Q → A: Reduces catalytic activity. 1 Publication
    Mutagenesisi495 – 4951Q → E: No effect on catalytic activity. 1 Publication
    Mutagenesisi499 – 4991H → Q: Inactive.
    Mutagenesisi504 – 5041H → Q or S: Inactive.
    Mutagenesisi517 – 5171H → Q: 33% of wild-type activity.
    Mutagenesisi522 – 5221H → Q: 1% of wild-type activity.
    Mutagenesisi531 – 5311H → Q: 20% of wild-type activity.
    Mutagenesisi542 – 5421A → G: Changes reaction profile to produce almost equal amounts of 13S- and 9R-hydroperoxyoctadecadienoate. 1 Publication
    Mutagenesisi542 – 5421A → S: Little effect on reaction profile. 1 Publication
    Mutagenesisi542 – 5421A → T or V: Complete loss of activity. 1 Publication
    Mutagenesisi690 – 6901H → Q: Inactive.
    Mutagenesisi697 – 6971Q → N or E: Reduces catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 839839Seed linoleate 13S-lipoxygenase-1PRO_0000220717Add
    BLAST

    Expressioni

    Inductioni

    The hydroperoxide product serves to activate the resting enzyme. The activation is accompanied by the oxidation of Fe2+entadiene structure. L-1 prefers anionic substrate.

    Gene expression databases

    GenevestigatoriP08170.

    Interactioni

    Subunit structurei

    Monomer.3 Publications

    Structurei

    Secondary structure

    1
    839
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 1610
    Helixi17 – 193
    Helixi24 – 263
    Helixi32 – 354
    Turni36 – 394
    Beta strandi40 – 5011
    Beta strandi54 – 585
    Beta strandi66 – 683
    Beta strandi79 – 868
    Helixi89 – 913
    Beta strandi94 – 1018
    Beta strandi103 – 1053
    Beta strandi107 – 1148
    Turni117 – 1204
    Beta strandi123 – 1319
    Helixi134 – 1363
    Beta strandi141 – 1444
    Helixi151 – 1533
    Helixi156 – 1583
    Helixi159 – 17012
    Turni195 – 1973
    Helixi199 – 2013
    Beta strandi206 – 2127
    Helixi242 – 2443
    Helixi251 – 2533
    Helixi255 – 2573
    Helixi258 – 2647
    Helixi266 – 27510
    Helixi286 – 2905
    Helixi291 – 2933
    Helixi301 – 3077
    Helixi313 – 3153
    Beta strandi317 – 3193
    Beta strandi321 – 3266
    Helixi331 – 3333
    Helixi339 – 3413
    Helixi343 – 35210
    Beta strandi353 – 3553
    Beta strandi364 – 3663
    Helixi373 – 3764
    Helixi385 – 3873
    Helixi395 – 4006
    Beta strandi404 – 4085
    Helixi410 – 42112
    Beta strandi430 – 4378
    Beta strandi443 – 4519
    Beta strandi465 – 4673
    Helixi473 – 49624
    Helixi497 – 5037
    Helixi504 – 51714
    Helixi523 – 5286
    Helixi529 – 5324
    Helixi535 – 54511
    Helixi552 – 5565
    Helixi560 – 5623
    Helixi563 – 5719
    Helixi576 – 5794
    Helixi581 – 5877
    Beta strandi590 – 5934
    Beta strandi600 – 6056
    Helixi609 – 62820
    Helixi629 – 6313
    Helixi636 – 6405
    Helixi643 – 65412
    Turni655 – 6573
    Helixi658 – 6603
    Beta strandi669 – 6713
    Helixi672 – 68615
    Helixi688 – 6947
    Helixi697 – 7015
    Turni704 – 7063
    Helixi721 – 7288
    Helixi730 – 7378
    Helixi741 – 75414
    Helixi776 – 80126
    Helixi803 – 8053
    Helixi806 – 8094
    Turni810 – 8145
    Beta strandi826 – 8283
    Beta strandi834 – 8363

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F8NX-ray1.40A1-839[»]
    1FGMX-ray1.90A1-839[»]
    1FGOX-ray1.62A1-839[»]
    1FGQX-ray1.85A1-839[»]
    1FGRX-ray1.60A1-839[»]
    1FGTX-ray1.62A1-839[»]
    1Y4KX-ray1.95A1-839[»]
    1YGEX-ray1.40A1-839[»]
    2SBLX-ray2.60A/B1-839[»]
    3BNBX-ray1.45A1-839[»]
    3BNCX-ray1.65A1-839[»]
    3BNDX-ray1.60A1-839[»]
    3BNEX-ray1.40A1-839[»]
    3PZWX-ray1.40A1-839[»]
    ProteinModelPortaliP08170.
    SMRiP08170. Positions 1-839.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08170.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 145130PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini148 – 839692LipoxygenasePROSITE-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

    Phylogenomic databases

    KOiK15718.

    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.

    P08170-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFSAGHKIKG TVVLMPKNEL EVNPDGSAVD NLNAFLGRSV SLQLISATKA    50
    DAHGKGKVGK DTFLEGINTS LPTLGAGESA FNIHFEWDGS MGIPGAFYIK 100
    NYMQVEFFLK SLTLEAISNQ GTIRFVCNSW VYNTKLYKSV RIFFANHTYV 150
    PSETPAPLVS YREEELKSLR GNGTGERKEY DRIYDYDVYN DLGNPDKSEK 200
    LARPVLGGSS TFPYPRRGRT GRGPTVTDPN TEKQGEVFYV PRDENLGHLK 250
    SKDALEIGTK SLSQIVQPAF ESAFDLKSTP IEFHSFQDVH DLYEGGIKLP 300
    RDVISTIIPL PVIKELYRTD GQHILKFPQP HVVQVSQSAW MTDEEFAREM 350
    IAGVNPCVIR GLEEFPPKSN LDPAIYGDQS SKITADSLDL DGYTMDEALG 400
    SRRLFMLDYH DIFMPYVRQI NQLNSAKTYA TRTILFLRED GTLKPVAIEL 450
    SLPHSAGDLS AAVSQVVLPA KEGVESTIWL LAKAYVIVND SCYHQLMSHW 500
    LNTHAAMEPF VIATHRHLSV LHPIYKLLTP HYRNNMNINA LARQSLINAN 550
    GIIETTFLPS KYSVEMSSAV YKNWVFTDQA LPADLIKRGV AIKDPSTPHG 600
    VRLLIEDYPY AADGLEIWAA IKTWVQEYVP LYYARDDDVK NDSELQHWWK 650
    EAVEKGHGDL KDKPWWPKLQ TLEDLVEVCL IIIWIASALH AAVNFGQYPY 700
    GGLIMNRPTA SRRLLPEKGT PEYEEMINNH EKAYLRTITS KLPTLISLSV 750
    IEILSTHASD EVYLGQRDNP HWTSDSKALQ AFQKFGNKLK EIEEKLVRRN 800
    NDPSLQGNRL GPVQLPYTLL YPSSEEGLTF RGIPNSISI 839
    Length:839
    Mass (Da):94,369
    Last modified:August 1, 1992 - v2
    Checksum:i1586250ACD3E34A4
    GO

    Sequence cautioni

    The sequence CAA47717.1 differs from that shown. Reason: Frameshift at positions 663 and 697.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti426 – 4272AK → RN1 PublicationCurated
    Sequence conflicti558 – 5603LPS → AL1 PublicationCurated
    Sequence conflicti572 – 5743KNW → EL1 PublicationCurated
    Sequence conflicti641 – 6411N → P1 PublicationCurated
    Sequence conflicti741 – 7488KLPTLISL → SCRLSLAV1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02795 mRNA. Translation: AAA33986.1.
    X67304 mRNA. Translation: CAA47717.1. Frameshift.
    PIRiS25064. DASYL2.
    RefSeqiNP_001236153.1. NM_001249224.1.
    UniGeneiGma.947.

    Genome annotation databases

    GeneIDi547923.
    KEGGigmx:547923.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02795 mRNA. Translation: AAA33986.1 .
    X67304 mRNA. Translation: CAA47717.1 . Frameshift.
    PIRi S25064. DASYL2.
    RefSeqi NP_001236153.1. NM_001249224.1.
    UniGenei Gma.947.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F8N X-ray 1.40 A 1-839 [» ]
    1FGM X-ray 1.90 A 1-839 [» ]
    1FGO X-ray 1.62 A 1-839 [» ]
    1FGQ X-ray 1.85 A 1-839 [» ]
    1FGR X-ray 1.60 A 1-839 [» ]
    1FGT X-ray 1.62 A 1-839 [» ]
    1Y4K X-ray 1.95 A 1-839 [» ]
    1YGE X-ray 1.40 A 1-839 [» ]
    2SBL X-ray 2.60 A/B 1-839 [» ]
    3BNB X-ray 1.45 A 1-839 [» ]
    3BNC X-ray 1.65 A 1-839 [» ]
    3BND X-ray 1.60 A 1-839 [» ]
    3BNE X-ray 1.40 A 1-839 [» ]
    3PZW X-ray 1.40 A 1-839 [» ]
    ProteinModelPortali P08170.
    SMRi P08170. Positions 1-839.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P08170.
    ChEMBLi CHEMBL4586.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 547923.
    KEGGi gmx:547923.

    Phylogenomic databases

    KOi K15718.

    Enzyme and pathway databases

    UniPathwayi UPA00382 .
    SABIO-RK P08170.

    Miscellaneous databases

    EvolutionaryTracei P08170.

    Gene expression databases

    Genevestigatori P08170.

    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. "Primary structure of soybean lipoxygenase-1."
      Shibata D., Steczko J., Dixon J.E., Hermodson M., Yazdanparast R., Axelrod B.
      J. Biol. Chem. 262:10080-10085(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. Fukazawa C., Masayoshi M., Chikafusa F.
      Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Bonminori.
      Tissue: Cotyledon.
    3. "Two soybean seed lipoxygenase nulls accumulate reduced levels of lipoxygenase transcripts."
      Start W.G., Ma Y., Polacco J.C., Hildebrand D.F., Freyer G.A., Altschuler M.
      Plant Mol. Biol. 7:11-23(1986)
      [AGRICOLA] [Europe PMC]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 426-752.
    4. "Conserved histidine residues in soybean lipoxygenase: functional consequences of their replacement."
      Steczko J., Donoho G.P., Clemens J.C., Dixon J.E., Axelrod B.
      Biochemistry 31:4053-4057(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 479-482, MUTAGENESIS OF SOME HISTIDINE RESIDUES.
    5. "Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-hydroperoxides from linoleic acid by a pH-dependent mechanism."
      Gardner H.W.
      Biochim. Biophys. Acta 1001:274-281(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SPECIFICITY.
    6. "Identification of the iron-binding histidine residues in soybean lipoxygenase L-1."
      Steczko J., Axelrod B.
      Biochem. Biophys. Res. Commun. 186:686-689(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SOME HISTIDINE RESIDUES.
    7. "Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1."
      Minor W., Steczko J., Bolin J.T., Otwinowski Z., Axelrod B.
      Biochemistry 32:6320-6323(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR.
    8. "On the relationships of substrate orientation, hydrogen abstraction, and product stereochemistry in single and double dioxygenations by soybean lipoxygenase-1 and its Ala542Gly mutant."
      Coffa G., Imber A.N., Maguire B.C., Laxmikanthan G., Schneider C., Gaffney B.J., Brash A.R.
      J. Biol. Chem. 280:38756-38766(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ALA-542, ENZYME KINETICS, REACTION MECHANISM, EPR SPECTROSCOPY.
    9. "The three-dimensional structure of an arachidonic acid 15-lipoxygenase."
      Boyington J.C., Gaffney B.J., Amzel L.M.
      Science 260:1482-1486(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH IRON IONS.
    10. "Crystal structure of soybean lipoxygenase L-1 at 1.4-A resolution."
      Minor W., Steczko J., Stec B., Otwinowski Z., Bolin J.T., Walter R., Axelrod B.
      Biochemistry 35:10687-10701(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH IRON IONS.
    11. "Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1."
      Tomchick D.R., Phan P., Cymborowski M., Minor W., Holman T.R.
      Biochemistry 40:7509-7517(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF WILD-TYPE AND MUTANTS GLN-495 AND GLN-697 IN COMPLEX WITH IRON IONS, MUTAGENESIS OF GLN-495 AND GLN-697.

    Entry informationi

    Entry nameiLOX1_SOYBN
    AccessioniPrimary (citable) accession number: P08170
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Soybean contains at least 4 distinct isoenzymes, L-1, L-2, L-3a and L-3b in dry seeds, and at least two distinct isozymes in the hypocotyl/radicle region of the seedling stem.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3