ID   LOX2_PEA                Reviewed;         864 AA.
AC   P14856;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Seed linoleate 9S-lipoxygenase-2;
DE            EC=1.13.11.58;
DE   AltName: Full=Lipoxygenase-2;
GN   Name=LOX1.2;
OS   Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Birte;
RX   PubMed=2515855; DOI=10.1042/bj2640929;
RA   Ealing P.M., Casey R.;
RT   "The cDNA cloning of a pea (Pisum sativum) seed lipoxygenase. Sequence
RT   comparisons of the two major pea seed lipoxygenase isoforms.";
RL   Biochem. J. 264:929-932(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Birte;
RA   Casey R.;
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|PROSITE-
CC       ProRule:PRU00726};
CC   -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC       ProRule:PRU00726}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR   EMBL; X17061; CAA34906.1; -; mRNA.
DR   EMBL; X78580; CAA55318.1; -; Genomic_DNA.
DR   PIR; S07075; S07075.
DR   AlphaFoldDB; P14856; -.
DR   SMR; P14856; -.
DR   BRENDA; 1.13.11.B6; 4872.
DR   UniPathway; UPA00382; -.
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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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.
FT   CHAIN           1..864
FT                   /note="Seed linoleate 9S-lipoxygenase-2"
FT                   /id="PRO_0000220713"
FT   DOMAIN          46..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          230..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         524
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         529
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         716
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         720
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         864
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   CONFLICT        333
FT                   /note="L -> I (in Ref. 2; CAA55318)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        562
FT                   /note="Missing (in Ref. 2; CAA55318)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        578
FT                   /note="L -> I (in Ref. 2; CAA55318)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   864 AA;  97134 MW;  2919AF5FAF272CDF CRC64;
     MFPNVTGLLN KGHKIRGTVV LMRKNVLDFN TIVSIGGGNV HGVIDSGINI IGSTLDGLTA
     FLGRSVSLQL ISATKSDANG KGKVGKDTFL EGVLASLPTL GAGESAFNIH FEWDHEMGIP
     GAFYIKNYMQ VEFFLKSLTL EDVPNHGTIR FVCNSWVYNS KLYKSPRIFF ANKSYLPSET
     PSPLVKYREE ELQTLRGDGT GERKLHERIY DYDVYNDLGN PDHGEHLARP ILGGSSTHPY
     PRRGRTGRYP TRKDPNSEKP ATETYVPRDE NFGHLKSSDF LAYGIKSVSQ CVVPAFESAF
     DLNFTPNEFD SFQDVRNLFE GGIKLPLDVI STLSPLPVVK EIFRTDGEQV LKFTPPHVIR
     VSKSAWMTDE EFAREMLAGV NPCMIRGLQE FPPKSNLDPA EYGDHTSKIS VDVLNLDGCT
     IDEALASGRL FILDYHDTFI PFLRRINETS AKAYATRTIL FLKENGTLKP VAIELSLPHP
     DGDKSGFVSK VILPADEGVE STIWLLAKAY VVVNDSCYHQ LMSHWLNTHA VIEPFVIATN
     RQLSVVHPIN KLLAPHYRDT MMNINALARD SLINANGLIE RSFLPSKYAV EMSSAVYKYW
     VFTDQALPND LIKRNMAVKD SSSPYGLRLL IEDYPYAVDG LEIWTAIKTW VQDYVSLYYA
     TDNDIKNDSE LQHWWKEVVE KGHGDLKDKP WWPKLQTFDE LVEVCTIIIW TASALHAAVN
     FGQYPYGGLI LNRPTLSRRL LPEEGTAEYD EMVKSSQKAY LRTITPKFQT LIDLSVIEIL
     SRHASDEVYL GQRENPHWTS DSKALQAFQK FGNKLAEIEA KLTNKNNDPS LYHRVGPVQL
     PYTLLHPSSK EGLTFRGIPN SISI