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P09186

- LOX3_SOYBN

UniProt

P09186 - LOX3_SOYBN

Protein

Seed linoleate 9S-lipoxygenase-3

Gene

LOX1.3

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 120 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.

    Catalytic activityi

    Linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate.

    Cofactori

    Binds 1 iron ion per subunit. Iron is tightly bound By similarity.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi518 – 5181Iron; catalytic
    Metal bindingi523 – 5231Iron; catalytic
    Metal bindingi709 – 7091Iron; catalytic
    Metal bindingi713 – 7131Iron; catalytic
    Metal bindingi857 – 8571Iron; via carboxylate; catalytic

    GO - Molecular functioni

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

    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:
    Seed linoleate 9S-lipoxygenase-3 (EC:1.13.11.58)
    Alternative name(s):
    Lipoxygenase-3
    Short name:
    L-3
    Gene namesi
    Name:LOX1.3
    Synonyms:LOX3
    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
    Mutagenesisi713 – 7131N → A or S: No loss of iron-binding; loss of catalytic activity. 1 Publication
    Mutagenesisi713 – 7131N → H: No loss of iron-binding; no change in catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 857857Seed linoleate 9S-lipoxygenase-3PRO_0000220719Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP09186.

    Interactioni

    Subunit structurei

    Monomer.5 Publications

    Structurei

    Secondary structure

    1
    857
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 2011
    Helixi21 – 233
    Turni26 – 305
    Turni39 – 413
    Beta strandi44 – 485
    Helixi50 – 534
    Beta strandi55 – 6814
    Beta strandi70 – 767
    Beta strandi84 – 863
    Turni89 – 913
    Beta strandi97 – 1004
    Beta strandi103 – 1053
    Beta strandi107 – 1093
    Beta strandi112 – 1198
    Beta strandi121 – 1233
    Beta strandi125 – 1339
    Beta strandi135 – 1373
    Beta strandi141 – 1499
    Helixi152 – 1543
    Beta strandi155 – 1573
    Beta strandi159 – 1624
    Turni169 – 1713
    Turni174 – 1763
    Helixi177 – 18812
    Helixi213 – 2153
    Helixi217 – 2193
    Beta strandi224 – 2307
    Beta strandi246 – 2505
    Helixi260 – 2623
    Helixi269 – 2713
    Helixi273 – 2786
    Turni279 – 2835
    Helixi284 – 29310
    Beta strandi294 – 2974
    Helixi304 – 3085
    Turni309 – 3135
    Helixi319 – 3246
    Turni325 – 3273
    Beta strandi328 – 3303
    Beta strandi332 – 3354
    Beta strandi339 – 3413
    Helixi349 – 3513
    Helixi357 – 3593
    Helixi361 – 37010
    Beta strandi371 – 3733
    Beta strandi382 – 3843
    Beta strandi390 – 3923
    Helixi393 – 3964
    Helixi403 – 4053
    Beta strandi408 – 4103
    Helixi415 – 4206
    Beta strandi424 – 4285
    Turni431 – 4333
    Helixi434 – 4363
    Helixi437 – 4415
    Turni442 – 4443
    Beta strandi449 – 4568
    Beta strandi462 – 47211
    Beta strandi474 – 4774
    Beta strandi482 – 4865
    Helixi492 – 51524
    Helixi516 – 5227
    Helixi523 – 53614
    Helixi542 – 5476
    Helixi548 – 5514
    Helixi554 – 56411
    Beta strandi566 – 5694
    Helixi571 – 5755
    Helixi579 – 5813
    Helixi582 – 5898
    Helixi590 – 5923
    Helixi595 – 5984
    Helixi600 – 6067
    Beta strandi609 – 6124
    Beta strandi619 – 6257
    Helixi628 – 65124
    Helixi656 – 6594
    Helixi662 – 67312
    Turni674 – 6763
    Helixi677 – 6793
    Beta strandi688 – 6903
    Helixi691 – 70515
    Helixi707 – 7137
    Helixi716 – 7205
    Turni723 – 7253
    Beta strandi730 – 7323
    Beta strandi737 – 7393
    Helixi740 – 7478
    Helixi749 – 7546
    Helixi760 – 77314
    Turni783 – 7853
    Helixi795 – 81824
    Helixi825 – 8273
    Turni828 – 8325
    Beta strandi844 – 8463
    Beta strandi852 – 8543

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HU9X-ray2.20A1-857[»]
    1IK3X-ray2.00A1-857[»]
    1JNQX-ray2.10A1-857[»]
    1LNHX-ray2.60A1-857[»]
    1N8QX-ray2.10A1-857[»]
    1NO3X-ray2.15A1-857[»]
    1ROVX-ray2.00A1-857[»]
    1RRHX-ray2.00A1-857[»]
    1RRLX-ray2.09A/B1-857[»]
    ProteinModelPortaliP09186.
    SMRiP09186. Positions 7-857.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09186.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 163126PLATPROSITE-ProRule annotationAdd
    BLAST
    Domaini166 – 857692LipoxygenasePROSITE-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.

    P09186-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGGLLHRGH KIKGTVVLMR KNVLHVNSVT SVGGIIGQGL DLVGSTLDTL    50
    TAFLGRPVSL QLISATKADA NGKGKLGKAT FLEGIITSLP TLGAGQSAFK 100
    INFEWDDGSG ILGAFYIKNF MQTEFFLVSL TLEDIPNHGS IHFVCNSWIY 150
    NAKLFKSDRI FFANQTYLPS ETPAPLVKYR EEELHNLRGD GTGERKEWER 200
    VYDYDVYNDL GDPDKGENHA RPVLGGNDTF PYPRRGRTGR KPTRKDPNSE 250
    SRSNDVYLPR DEAFGHLKSS DFLTYGLKSV SQNVLPLLQS AFDLNFTPRE 300
    FDSFDEVHGL YSGGIKLPTD IISKISPLPV LKEIFRTDGE QALKFPPPKV 350
    IQVSKSAWMT DEEFAREMLA GVNPNLIRCL KEFPPRSKLD SQVYGDHTSQ 400
    ITKEHLEPNL EGLTVDEAIQ NKRLFLLGHH DPIMPYLRRI NATSTKAYAT 450
    RTILFLKNDG TLRPLAIELS LPHPQGDQSG AFSQVFLPAD EGVESSIWLL 500
    AKAYVVVNDS CYHQLVSHWL NTHAVVEPFI IATNRHLSVV HPIYKLLHPH 550
    YRDTMNINGL ARLSLVNDGG VIEQTFLWGR YSVEMSAVVY KDWVFTDQAL 600
    PADLIKRGMA IEDPSCPHGI RLVIEDYPYA VDGLEIWDAI KTWVHEYVFL 650
    YYKSDDTLRE DPELQACWKE LVEVGHGDKK NEPWWPKMQT REELVEACAI 700
    IIWTASALHA AVNFGQYPYG GLILNRPTLS RRFMPEKGSA EYEELRKNPQ 750
    KAYLKTITPK FQTLIDLSVI EILSRHASDE VYLGERDNPN WTSDTRALEA 800
    FKRFGNKLAQ IENKLSERNN DEKLRNRCGP VQMPYTLLLP SSKEGLTFRG 850
    IPNSISI 857
    Length:857
    Mass (Da):96,758
    Last modified:July 1, 1989 - v1
    Checksum:i5DFC33D0F6FD32F0
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251H → D in strain: cv. Provar.
    Natural varianti57 – 571P → S in strain: cv. Provar.
    Natural varianti112 – 1121L → P in strain: cv. Provar.
    Natural varianti201 – 2011V → I in strain: cv. Provar.
    Natural varianti382 – 3821E → D in strain: cv. Provar.
    Natural varianti428 – 4281G → D in strain: cv. Provar.
    Natural varianti630 – 6301A → T in strain: cv. Provar.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06928 Genomic DNA. Translation: CAA30016.1.
    X13302 mRNA. Translation: CAA31664.1. Sequence problems.
    U50081 mRNA. Translation: AAB41272.1.
    PIRiS01864.
    RefSeqiNP_001235383.1. NM_001248454.1.
    UniGeneiGma.30739.

    Genome annotation databases

    GeneIDi547869.
    KEGGigmx:547869.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06928 Genomic DNA. Translation: CAA30016.1 .
    X13302 mRNA. Translation: CAA31664.1 . Sequence problems.
    U50081 mRNA. Translation: AAB41272.1 .
    PIRi S01864.
    RefSeqi NP_001235383.1. NM_001248454.1.
    UniGenei Gma.30739.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HU9 X-ray 2.20 A 1-857 [» ]
    1IK3 X-ray 2.00 A 1-857 [» ]
    1JNQ X-ray 2.10 A 1-857 [» ]
    1LNH X-ray 2.60 A 1-857 [» ]
    1N8Q X-ray 2.10 A 1-857 [» ]
    1NO3 X-ray 2.15 A 1-857 [» ]
    1ROV X-ray 2.00 A 1-857 [» ]
    1RRH X-ray 2.00 A 1-857 [» ]
    1RRL X-ray 2.09 A/B 1-857 [» ]
    ProteinModelPortali P09186.
    SMRi P09186. Positions 7-857.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 547869.
    KEGGi gmx:547869.

    Phylogenomic databases

    KOi K15718.

    Enzyme and pathway databases

    UniPathwayi UPA00382 .

    Miscellaneous databases

    EvolutionaryTracei P09186.

    Gene expression databases

    Genevestigatori P09186.

    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. "Isolation and characterization of a soybean (Glycine max) lipoxygenase-3 gene."
      Yenofsky R.L., Fine M., Liu C.
      Mol. Gen. Genet. 211:215-222(1988)
      Cited for: NUCLEOTIDE SEQUENCE.
    2. Yenofsky R.L.
      Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Position 713 is critical for catalysis but not iron binding in soybean lipoxygenase 3."
      Kramer J.A., Johnson K.R., Dunham W.R., Sands R.H., Funk M.O. Jr.
      Biochemistry 33:15017-15022(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE, MUTAGENESIS OF ASN-713.
      Strain: cv. Provar.
    4. "Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme."
      Skrzypczak-Jankun E., Amzel L.M., Kroa B.A., Funk M.O. Jr.
      Proteins 29:15-31(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
      Strain: cv. Provar.
    5. "Structural and thermochemical characterization of lipoxygenase-catechol complexes."
      Pham C., Jankun J., Skrzypczak-Jankun E., Flowers R.A., Funk M.O. Jr.
      Biochemistry 37:17952-17957(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
      Strain: cv. Provar.
    6. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON IONS AND SUBSTRATE.
      Strain: cv. Provar.
    7. "Structure of curcumin in complex with lipoxygenase and its significance in cancer."
      Skrzypczak-Jankun E., Zhou K., McCabe N.P., Selman S.H., Jankun J.
      Int. J. Mol. Med. 12:17-24(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH IRON IONS AND CURCUMIN.
    8. "Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead."
      Skrzypczak-Jankun E., Zhou K., Jankun J.
      Int. J. Mol. Med. 12:415-420(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH IRON IONS AND THE INHIBITOR EPIGALLO-CATECHIN.
    9. "Soybean lipoxygenase-3 in complex with 4-nitrocatechol."
      Skrzypczak-Jankun E., Borbulevych O.Y., Jankun J.
      Acta Crystallogr. D 60:613-615(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH IRON IONS AND 4-NITROCATECHOL.
    10. "Lipoxygenase interactions with natural flavonoid, quercetin, reveal a complex with protocatechuic acid in its X-ray structure at 2.1 A resolution."
      Borbulevych O.Y., Jankun J., Selman S.H., Skrzypczak-Jankun E.
      Proteins 54:13-19(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH IRON IONS AND PROTOCATECHUIC ACID.

    Entry informationi

    Entry nameiLOX3_SOYBN
    AccessioniPrimary (citable) accession number: P09186
    Secondary accession number(s): Q39838
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 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, 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