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P09186

- LOX3_SOYBN

UniProt

P09186 - LOX3_SOYBN

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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

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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

InParanoidiP09186.
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

        10         20         30         40         50
MLGGLLHRGH KIKGTVVLMR KNVLHVNSVT SVGGIIGQGL DLVGSTLDTL
60 70 80 90 100
TAFLGRPVSL QLISATKADA NGKGKLGKAT FLEGIITSLP TLGAGQSAFK
110 120 130 140 150
INFEWDDGSG ILGAFYIKNF MQTEFFLVSL TLEDIPNHGS IHFVCNSWIY
160 170 180 190 200
NAKLFKSDRI FFANQTYLPS ETPAPLVKYR EEELHNLRGD GTGERKEWER
210 220 230 240 250
VYDYDVYNDL GDPDKGENHA RPVLGGNDTF PYPRRGRTGR KPTRKDPNSE
260 270 280 290 300
SRSNDVYLPR DEAFGHLKSS DFLTYGLKSV SQNVLPLLQS AFDLNFTPRE
310 320 330 340 350
FDSFDEVHGL YSGGIKLPTD IISKISPLPV LKEIFRTDGE QALKFPPPKV
360 370 380 390 400
IQVSKSAWMT DEEFAREMLA GVNPNLIRCL KEFPPRSKLD SQVYGDHTSQ
410 420 430 440 450
ITKEHLEPNL EGLTVDEAIQ NKRLFLLGHH DPIMPYLRRI NATSTKAYAT
460 470 480 490 500
RTILFLKNDG TLRPLAIELS LPHPQGDQSG AFSQVFLPAD EGVESSIWLL
510 520 530 540 550
AKAYVVVNDS CYHQLVSHWL NTHAVVEPFI IATNRHLSVV HPIYKLLHPH
560 570 580 590 600
YRDTMNINGL ARLSLVNDGG VIEQTFLWGR YSVEMSAVVY KDWVFTDQAL
610 620 630 640 650
PADLIKRGMA IEDPSCPHGI RLVIEDYPYA VDGLEIWDAI KTWVHEYVFL
660 670 680 690 700
YYKSDDTLRE DPELQACWKE LVEVGHGDKK NEPWWPKMQT REELVEACAI
710 720 730 740 750
IIWTASALHA AVNFGQYPYG GLILNRPTLS RRFMPEKGSA EYEELRKNPQ
760 770 780 790 800
KAYLKTITPK FQTLIDLSVI EILSRHASDE VYLGERDNPN WTSDTRALEA
810 820 830 840 850
FKRFGNKLAQ IENKLSERNN DEKLRNRCGP VQMPYTLLLP SSKEGLTFRG

IPNSISI
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

InParanoidi P09186.
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: November 26, 2014
This is version 122 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