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P08170

- LOX1_SOYBN

UniProt

P08170 - LOX1_SOYBN

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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

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

Fe cation1 PublicationPROSITE-ProRule annotationNote: Binds 1 Fe cation 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
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

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-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

InParanoidiP08170.
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

        10         20         30         40         50
MFSAGHKIKG TVVLMPKNEL EVNPDGSAVD NLNAFLGRSV SLQLISATKA
60 70 80 90 100
DAHGKGKVGK DTFLEGINTS LPTLGAGESA FNIHFEWDGS MGIPGAFYIK
110 120 130 140 150
NYMQVEFFLK SLTLEAISNQ GTIRFVCNSW VYNTKLYKSV RIFFANHTYV
160 170 180 190 200
PSETPAPLVS YREEELKSLR GNGTGERKEY DRIYDYDVYN DLGNPDKSEK
210 220 230 240 250
LARPVLGGSS TFPYPRRGRT GRGPTVTDPN TEKQGEVFYV PRDENLGHLK
260 270 280 290 300
SKDALEIGTK SLSQIVQPAF ESAFDLKSTP IEFHSFQDVH DLYEGGIKLP
310 320 330 340 350
RDVISTIIPL PVIKELYRTD GQHILKFPQP HVVQVSQSAW MTDEEFAREM
360 370 380 390 400
IAGVNPCVIR GLEEFPPKSN LDPAIYGDQS SKITADSLDL DGYTMDEALG
410 420 430 440 450
SRRLFMLDYH DIFMPYVRQI NQLNSAKTYA TRTILFLRED GTLKPVAIEL
460 470 480 490 500
SLPHSAGDLS AAVSQVVLPA KEGVESTIWL LAKAYVIVND SCYHQLMSHW
510 520 530 540 550
LNTHAAMEPF VIATHRHLSV LHPIYKLLTP HYRNNMNINA LARQSLINAN
560 570 580 590 600
GIIETTFLPS KYSVEMSSAV YKNWVFTDQA LPADLIKRGV AIKDPSTPHG
610 620 630 640 650
VRLLIEDYPY AADGLEIWAA IKTWVQEYVP LYYARDDDVK NDSELQHWWK
660 670 680 690 700
EAVEKGHGDL KDKPWWPKLQ TLEDLVEVCL IIIWIASALH AAVNFGQYPY
710 720 730 740 750
GGLIMNRPTA SRRLLPEKGT PEYEEMINNH EKAYLRTITS KLPTLISLSV
760 770 780 790 800
IEILSTHASD EVYLGQRDNP HWTSDSKALQ AFQKFGNKLK EIEEKLVRRN
810 820 830
NDPSLQGNRL GPVQLPYTLL YPSSEEGLTF RGIPNSISI
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. Curated

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

InParanoidi P08170.
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: November 26, 2014
This is version 145 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