LOX2_SOYBN
ID LOX2_SOYBN Reviewed; 865 AA.
AC P09439;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Seed linoleate 9S-lipoxygenase-2;
DE EC=1.13.11.58;
DE AltName: Full=Lipoxygenase-2;
DE Short=L-2;
GN Name=LOX1.2; Synonyms=LOX2;
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 [MRNA].
RX PubMed=2834391; DOI=10.1016/s0021-9258(18)68716-2;
RA Shibata D., Steczko J., Dixon J.E., Andrews P.C., Hermodson M., Axelrod B.;
RT "Primary structure of soybean lipoxygenase L-2.";
RL J. Biol. Chem. 263:6816-6821(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-865.
RX AGRICOLA=IND87003970; DOI=10.1007/BF00020127;
RA Start W.G., Ma Y., Polacco J.C., Hildebrand D.F., Freyer G.A.,
RA Altschuler M.;
RT "Two soybean seed lipoxygenase nulls accumulate reduced levels of
RT lipoxygenase transcripts.";
RL Plant Mol. Biol. 7:11-23(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 859-865.
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).
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 Evidence={ECO:0000255|PROSITE-ProRule:PRU00726};
CC Note=Binds 1 Fe cation per subunit. Iron is tightly bound.
CC {ECO:0000255|PROSITE-ProRule:PRU00726};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J03211; AAA33987.1; -; mRNA.
DR EMBL; X56139; CAA39605.1; -; Genomic_DNA.
DR PIR; A28161; DASYL1.
DR AlphaFoldDB; P09439; -.
DR SMR; P09439; -.
DR STRING; 3847.GLYMA13G42310.1; -.
DR PRIDE; P09439; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR InParanoid; P09439; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cytoplasm; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Reference proteome.
FT CHAIN 1..865
FT /note="Seed linoleate 9S-lipoxygenase-2"
FT /id="PRO_0000220718"
FT DOMAIN 50..175
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 178..865
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 234..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 527
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 532
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 718
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 722
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 865
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT CONFLICT 263..264
FT /note="KP -> NL (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="D -> Y (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="L -> P (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="L -> H (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="D -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="V -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="V -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 865 AA; 97146 MW; 74CBD32E3E4A0C85 CRC64;
MFSVPGVSGI LNRGGGHKIK GTVVLMRKNV LDFNSVADLT KGNVGGLIGT GLNVVGSTLD
NLTAFLGRSV ALQLISATKP LANGKGKVGK DTFLEGIIVS LPTLGAGESA FNIQFEWDES
MGIPGAFYIK NYMQVEFYLK SLTLEDVPNQ GTIRFVCNSW VYNTKLYKSV RIFFANHTYV
PSETPAALVG YREEELKNLR GDGKGERKEH DRIYDYDVYN DLGNPDHGEN FARPILGGSS
THPYPRRGRT GRYPTRKDQN SEKPGEVYVP RDENFGHLKS SDFLAYGIKS LSQYVLPAFE
SVFDLNFTPN EFDSFQDVRD LHEGGIKLPT EVISTIMPLP VVKELFRTDG EQVLKFPPPH
VIQVSKSAWM TDEEFAREMV AGVNPCVIRG LQEFPPKSNL DPTIYGEQTS KITADALDLD
GYTVDEALAS RRLFMLDYHD VFMPYIRRIN QTYAKAYATR TILFLRENGT LKPVAIELSL
PHPAGDLSGA VSQVILPAKE GVESTIWLLA KAYVVVNDSC YHQLMSHWLN THAVIEPFII
ATNRHLSALH PIYKLLTPHY RDTMNINALA RQSLINADGI IEKSFLPSKH SVEMSSAVYK
NWVFTDQALP ADLIKRGVAI KDPSAPHGLR LLIEDYPYAV DGLEIWAAIK TWVQEYVSLY
YARDDDVKPD SELQQWWKEA VEKGHGDLKD KPWWPKLQTI EELVEICTII IWTASALHAA
VNFGQYPYGG FILNRPTSSR RLLPEKGTPE YEEMVKSHQK AYLRTITSKF QTLVDLSVIE
ILSRHASDEV YLGQRDNPHW TSDSKALQAF QKFGNKLKEI EEKLARKNND QSLSNRLGPV
QLPYTLLHPN SEGLTCRGIP NSISI
