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Protein

Seed linoleate 13S-lipoxygenase-1

Gene

LOX1.1

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed-Annotation score: -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

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.

Catalytic activityi

Linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate.2 Publications
Alpha-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate.2 Publications

Cofactori

Fe cationPROSITE-ProRule annotation1 PublicationNote: Binds 1 Fe cation per subunit. Iron is tightly bound.PROSITE-ProRule annotation1 Publication

pH dependencei

Inactive below pH 6.0.1 Publication

Pathwayi: oxylipin biosynthesis

This protein is involved in the pathway oxylipin biosynthesis, which is part of Lipid metabolism.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway oxylipin biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi499Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi504Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi690Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi694Iron; catalytic1
Metal bindingi839Iron; via carboxylate; catalytic1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDioxygenase, Oxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Oxylipin biosynthesis
LigandIron, Metal-binding

Enzyme and pathway databases

SABIO-RKiP08170
UniPathwayiUPA00382

Chemistry databases

SwissLipidsiSLP:000001639

Names & Taxonomyi

Protein namesi
Recommended name:
Seed linoleate 13S-lipoxygenase-1 (EC:1.13.11.122 Publications)
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
Proteomesi
  • UP000008827 Componenti: Unplaced

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi494H → Q: 37% of wild-type activity. 1
Mutagenesisi494H → S: 8% of wild-type activity. 1
Mutagenesisi495Q → A: Reduces catalytic activity. 1 Publication1
Mutagenesisi495Q → E: No effect on catalytic activity. 1 Publication1
Mutagenesisi499H → Q: Inactive. 1
Mutagenesisi504H → Q or S: Inactive. 1
Mutagenesisi517H → Q: 33% of wild-type activity. 1
Mutagenesisi522H → Q: 1% of wild-type activity. 1
Mutagenesisi531H → Q: 20% of wild-type activity. 1
Mutagenesisi542A → G: Changes reaction profile to produce almost equal amounts of 13S- and 9R-hydroperoxyoctadecadienoate. 1 Publication1
Mutagenesisi542A → S: Little effect on reaction profile. 1 Publication1
Mutagenesisi542A → T or V: Complete loss of activity. 1 Publication1
Mutagenesisi690H → Q: Inactive. 1
Mutagenesisi697Q → N or E: Reduces catalytic activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4586

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002207171 – 839Seed linoleate 13S-lipoxygenase-1Add BLAST839

Proteomic databases

PRIDEiP08170

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.

Interactioni

Subunit structurei

Monomer.3 Publications

Protein-protein interaction databases

STRINGi3847.GLYMA13G42320.1

Chemistry databases

BindingDBiP08170

Structurei

Secondary structure

1839
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 16Combined sources10
Helixi17 – 19Combined sources3
Helixi24 – 26Combined sources3
Helixi32 – 35Combined sources4
Beta strandi39 – 50Combined sources12
Beta strandi56 – 58Combined sources3
Beta strandi66 – 68Combined sources3
Beta strandi79 – 86Combined sources8
Helixi89 – 91Combined sources3
Beta strandi94 – 101Combined sources8
Beta strandi103 – 105Combined sources3
Beta strandi107 – 114Combined sources8
Helixi119 – 121Combined sources3
Beta strandi123 – 131Combined sources9
Helixi134 – 136Combined sources3
Beta strandi141 – 144Combined sources4
Helixi151 – 153Combined sources3
Helixi156 – 158Combined sources3
Helixi159 – 170Combined sources12
Turni195 – 197Combined sources3
Helixi199 – 201Combined sources3
Beta strandi206 – 212Combined sources7
Helixi242 – 244Combined sources3
Helixi251 – 253Combined sources3
Helixi255 – 257Combined sources3
Helixi258 – 264Combined sources7
Helixi266 – 275Combined sources10
Helixi286 – 290Combined sources5
Helixi291 – 293Combined sources3
Helixi301 – 307Combined sources7
Helixi313 – 316Combined sources4
Beta strandi317 – 319Combined sources3
Beta strandi321 – 326Combined sources6
Helixi331 – 333Combined sources3
Helixi339 – 341Combined sources3
Helixi343 – 352Combined sources10
Beta strandi353 – 355Combined sources3
Beta strandi364 – 366Combined sources3
Helixi373 – 376Combined sources4
Helixi385 – 387Combined sources3
Helixi395 – 400Combined sources6
Beta strandi404 – 408Combined sources5
Helixi410 – 421Combined sources12
Beta strandi430 – 437Combined sources8
Beta strandi443 – 451Combined sources9
Beta strandi456 – 458Combined sources3
Beta strandi465 – 467Combined sources3
Helixi473 – 496Combined sources24
Helixi497 – 503Combined sources7
Helixi504 – 517Combined sources14
Helixi523 – 528Combined sources6
Helixi529 – 532Combined sources4
Helixi535 – 545Combined sources11
Helixi552 – 556Combined sources5
Helixi560 – 562Combined sources3
Helixi563 – 571Combined sources9
Helixi576 – 579Combined sources4
Helixi581 – 587Combined sources7
Beta strandi590 – 593Combined sources4
Beta strandi600 – 605Combined sources6
Helixi609 – 628Combined sources20
Helixi629 – 631Combined sources3
Helixi636 – 640Combined sources5
Helixi643 – 654Combined sources12
Turni655 – 657Combined sources3
Helixi658 – 660Combined sources3
Beta strandi669 – 671Combined sources3
Helixi672 – 686Combined sources15
Helixi688 – 694Combined sources7
Helixi697 – 701Combined sources5
Turni704 – 706Combined sources3
Beta strandi718 – 720Combined sources3
Helixi721 – 728Combined sources8
Helixi730 – 737Combined sources8
Helixi741 – 754Combined sources14
Helixi776 – 801Combined sources26
Helixi803 – 805Combined sources3
Helixi806 – 809Combined sources4
Turni810 – 814Combined sources5
Beta strandi826 – 828Combined sources3
Beta strandi834 – 836Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4WFOX-ray1.14A1-839[»]
4WHAX-ray1.70A1-839[»]
5EEOX-ray2.10A1-839[»]
5T5VX-ray1.80A/B1-839[»]
5TQNX-ray1.80A/B1-839[»]
5TQOX-ray1.70A/B1-839[»]
5TQPX-ray1.70A/B1-839[»]
5TR0X-ray1.85A/B1-839[»]
ProteinModelPortaliP08170
SMRiP08170
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08170

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 145PLATPROSITE-ProRule annotationAdd BLAST130
Domaini148 – 839LipoxygenasePROSITE-ProRule annotationAdd BLAST692

Sequence similaritiesi

Belongs to the lipoxygenase family.Curated

Phylogenomic databases

InParanoidiP08170
KOiK15718

Family and domain databases

Gene3Di4.10.372.101 hit
InterProiView protein in InterPro
IPR000907 LipOase
IPR013819 LipOase_C
IPR036226 LipOase_C_sf
IPR020834 LipOase_CS
IPR020833 LipOase_Fe_BS
IPR001246 LipOase_plant
IPR027433 Lipoxygenase_dom_3
IPR001024 PLAT/LH2_dom
IPR036392 PLAT/LH2_dom_sf
PANTHERiPTHR11771 PTHR11771, 1 hit
PfamiView protein in Pfam
PF00305 Lipoxygenase, 1 hit
PF01477 PLAT, 1 hit
PRINTSiPR00087 LIPOXYGENASE
PR00468 PLTLPOXGNASE
SMARTiView protein in SMART
SM00308 LH2, 1 hit
SUPFAMiSSF48484 SSF48484, 1 hit
SSF49723 SSF49723, 1 hit
PROSITEiView protein in PROSITE
PS00711 LIPOXYGENASE_1, 1 hit
PS00081 LIPOXYGENASE_2, 1 hit
PS51393 LIPOXYGENASE_3, 1 hit
PS50095 PLAT, 1 hit

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 differs from that shown. Reason: Frameshift at positions 663 and 697.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti426 – 427AK → RN (Ref. 3) Curated2
Sequence conflicti558 – 560LPS → AL (Ref. 3) Curated3
Sequence conflicti572 – 574KNW → EL (Ref. 3) Curated3
Sequence conflicti641N → P (Ref. 3) Curated1
Sequence conflicti741 – 748KLPTLISL → SCRLSLAV (Ref. 3) Curated8

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

Similar proteinsi

Entry informationi

Entry nameiLOX1_SOYBN
AccessioniPrimary (citable) accession number: P08170
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1992
Last modified: March 28, 2018
This is version 165 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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