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P09186

- LOX3_SOYBN

UniProt

P09186 - LOX3_SOYBN

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Protein
Seed linoleate 9S-lipoxygenase-3
Gene
LOX1.3, LOX3
Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

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
Complete GO annotation...

GO - Biological processi

  1. oxylipin biosynthetic process Source: UniProtKB-UniPathway
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:
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
Complete GO annotation...

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-3
PRO_0000220719Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP09186.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP09186.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 163126PLAT
Add
BLAST
Domaini166 – 857692Lipoxygenase
Add
BLAST

Sequence similaritiesi

Belongs to the lipoxygenase family.
Contains 1 PLAT domain.

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...

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: September 3, 2014
This is version 119 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

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