LOXX_SOYBN
ID LOXX_SOYBN Reviewed; 864 AA.
AC P24095;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Seed linoleate 9S-lipoxygenase;
DE EC=1.13.11.58;
DE AltName: Full=Lipoxygenase;
GN Name=LOX1.4; Synonyms=SC514;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Cotyledon;
RX PubMed=1909908; DOI=10.1007/bf00020569;
RA Shibata D., Kato T., Tanaka K.;
RT "Nucleotide sequences of a soybean lipoxygenase gene and the short
RT intergenic region between an upstream lipoxygenase gene.";
RL Plant Mol. Biol. 16:353-359(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Williams 82; TISSUE=Radicle;
RA Park T., Holland M.A., Laskey J.G., Polacco J.C.;
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON IONS.
RX PubMed=17022084; DOI=10.1002/prot.21182;
RA Youn B., Sellhorn G.E., Mirchel R.J., Gaffney B.J., Grimes H.D., Kang C.;
RT "Crystal structures of vegetative soybean lipoxygenase VLX-B and VLX-D, and
RT comparisons with seed isoforms LOX-1 and LOX-3.";
RL Proteins 65:1008-1020(2006).
CC -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse
CC aspects of plant physiology including growth and development, pest
CC resistance, and senescence or responses to wounding. It catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 1 Fe cation per subunit. Iron is tightly bound.;
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17022084}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Germinated cotyledons.
CC -!- INDUCTION: By jasmonate.
CC -!- MISCELLANEOUS: Soybean contains at least 4 distinct isoenzymes, L-1, L-
CC 2, L-3a and L-3b in dry seeds, and at least two distinct isozymes in
CC the hypocotyl/radicle region of the seedling stem.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; X56139; CAA39604.1; -; Genomic_DNA.
DR EMBL; U04526; AAA03728.1; -; mRNA.
DR PIR; S13381; S13381.
DR RefSeq; NP_001238676.1; NM_001251747.1.
DR PDB; 2IUK; X-ray; 2.40 A; A/B=1-864.
DR PDBsum; 2IUK; -.
DR AlphaFoldDB; P24095; -.
DR SMR; P24095; -.
DR STRING; 3847.GLYMA07G00900.1; -.
DR BindingDB; P24095; -.
DR ChEMBL; CHEMBL3120043; -.
DR PRIDE; P24095; -.
DR ProMEX; P24095; -.
DR EnsemblPlants; KRH47067; KRH47067; GLYMA_07G007000.
DR GeneID; 547835; -.
DR Gramene; KRH47067; KRH47067; GLYMA_07G007000.
DR KEGG; gmx:547835; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR InParanoid; P24095; -.
DR OMA; KHELWWP; -.
DR OrthoDB; 385042at2759; -.
DR UniPathway; UPA00382; -.
DR EvolutionaryTrace; P24095; -.
DR PRO; PR:P24095; -.
DR Proteomes; UP000008827; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01751; PLAT_LH2; 1.
DR Gene3D; 4.10.372.10; -; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001246; LipOase_plant.
DR InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR InterPro; IPR027433; Lipoxygenase_dom_3.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; PTHR11771; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00468; PLTLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Dioxygenase; Fatty acid biosynthesis;
KW Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Oxylipin biosynthesis; Reference proteome.
FT CHAIN 1..864
FT /note="Seed linoleate 9S-lipoxygenase"
FT /id="PRO_0000220721"
FT DOMAIN 44..171
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 174..864
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 244..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 525
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 530
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 716
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 720
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 864
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT CONFLICT 233
FT /note="S -> C (in Ref. 2; AAA03728)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="R -> L (in Ref. 2; AAA03728)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="D -> H (in Ref. 2; AAA03728)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="M -> K (in Ref. 2; AAA03728)"
FT /evidence="ECO:0000305"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:2IUK"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 290..298
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:2IUK"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 325..331
FT /evidence="ECO:0007829|PDB:2IUK"
FT TURN 335..340
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 367..376
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:2IUK"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 421..426
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 436..439
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 443..447
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 469..478
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 481..486
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 501..522
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 523..529
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 530..543
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 549..554
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 555..558
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 561..571
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 578..582
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 589..597
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 607..613
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 626..632
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 635..658
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 662..667
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 669..680
FT /evidence="ECO:0007829|PDB:2IUK"
FT TURN 681..683
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 698..712
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 714..720
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 723..727
FT /evidence="ECO:0007829|PDB:2IUK"
FT TURN 730..732
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 747..754
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 756..761
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 767..780
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 802..825
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 832..834
FT /evidence="ECO:0007829|PDB:2IUK"
FT HELIX 836..838
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 851..853
FT /evidence="ECO:0007829|PDB:2IUK"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:2IUK"
SQ SEQUENCE 864 AA; 96817 MW; 66F31FB1FA5F3B60 CRC64;
MFGIFDKGQK IKGTVVLMPK NVLDFNAITS IGKGGVIDTA TGILGQGVSL VGGVIDTATS
FLGRNISMQL ISATQTDGSG NGKVGKEVYL EKHLPTLPTL GARQDAFSIF FEWDASFGIP
GAFYIKNFMT DEFFLVSVKL EDIPNHGTIE FVCNSWVYNF RSYKKNRIFF VNDTYLPSAT
PAPLLKYRKE ELEVLRGDGT GKRKDFDRIY DYDVYNDLGN PDGGDPRPIL GGSSIYPYPR
RVRTGRERTR TDPNSEKPGE VYVPRDENFG HLKSSDFLTY GIKSLSHDVI PLFKSAIFQL
RVTSSEFESF EDVRSLYEGG IKLPTDILSQ ISPLPALKEI FRTDGENVLQ FPPPHVAKVS
KSGWMTDEEF AREVIAGVNP NVIRRLQEFP PKSTLDPTLY GDQTSTITKE QLEINMGGVT
VEEALSTQRL FILDYQDAFI PYLTRINSLP TAKAYATRTI LFLKDDGTLK PLAIELSKPH
PDGDNLGPES IVVLPATEGV DSTIWLLAKA HVIVNDSGYH QLVSHWLNTH AVMEPFAIAT
NRHLSVLHPI YKLLYPHYRD TININGLARQ SLINADGIIE KSFLPGKYSI EMSSSVYKNW
VFTDQALPAD LVKRGLAIED PSAPHGLRLV IEDYPYAVDG LEIWDAIKTW VHEYVSLYYP
TDAAVQQDTE LQAWWKEAVE KGHGDLKEKP WWPKMQTTED LIQSCSIIVW TASALHAAVN
FGQYPYGGLI LNRPTLARRF IPAEGTPEYD EMVKNPQKAY LRTITPKFET LIDLSVIEIL
SRHASDEIYL GERETPNWTT DKKALEAFKR FGSKLTGIEG KINARNSDPS LRNRTGPVQL
PYTLLHRSSE EGLTFKGIPN SISI
