LOX1_LENCU
ID LOX1_LENCU Reviewed; 866 AA.
AC P38414;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Linoleate 9S-lipoxygenase;
DE EC=1.13.11.58;
DE AltName: Full=Lipoxygenase;
GN Name=LOX1.1;
OS Lens culinaris (Lentil) (Cicer lens).
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; Lens.
OX NCBI_TaxID=3864;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seedling shoot;
RX PubMed=8117753; DOI=10.1016/0005-2760(94)90275-5;
RA Hilbers M.P., Rossi A., Finazzi-Agro A., Veldink G.A., Vliegenthart J.F.G.;
RT "The primary structure of a lipoxygenase from the shoots of etiolated
RT lentil seedlings derived from its cDNA.";
RL Biochim. Biophys. Acta 1211:239-242(1994).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; X71344; CAA50483.1; -; mRNA.
DR AlphaFoldDB; P38414; -.
DR SMR; P38414; -.
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..866
FT /note="Linoleate 9S-lipoxygenase"
FT /id="PRO_0000220704"
FT DOMAIN 42..171
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 174..866
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 226..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 526
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 531
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 717
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 721
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 866
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 866 AA; 96639 MW; E3E5D00E84E3C89C CRC64;
MASLLFGRGQ KLKGTVILMQ KNVLDINALT AAQSPSGIIG GAFGVVGSIA GSIIDTATAF
LGRSVRLRLI SATVADASGK GKVSKEAFLE GLLTSIPTLG DKQSAFSVHF EWDSNMGTPG
AFYIENFMQG GEFFLVSLTL DDVPNVGSIK FACNSWIYND KKYQSDRIFF ANKTYLPSAT
PAPLVSYRQE ELKTLRGDGT GERQEWDRIY DYDVYNDLGA PDQKATLGRP VLGGSSTLPY
PRRGRTGRKK TVKEPQSESR SDTVYLPRDE AFGHVKSSDF LVYILKSASQ NIVPQLRSVV
TLQLNNPEFN TFEDVRSLYD GGIKLPTDVL SKISPIPLFS ELFRSDGEAA LKFPPPKVIQ
VDHSAWMTDE EFAREMIAGV NPHIIKEVLS FPIKSKLDSQ LYGDNTSKIT KEHLEPNLGG
VTVEGAIQTN RLFTPDHHDA LFPYLRKINA TATKAYATRT VLFLQDNGTL KPLAIELSTP
HPDGDSFGPV SKVYLPASEG VEASIWLLAK AFVVVNDSCY HQLVSHWLNT HAVVEPFIIA
TNRHLSVVHP IHKLLLPHYR DTMNINALAR NVLVNAEGII ESTFLWGNYA MEMSAVVYKD
WVFPDQGLPN DLIKRGVAVK DPSSPHGVRL LIEDYPYASD GLEIWAAIKS WVEEYVNFYY
KSDAAIAQDA ELQAFWKELV EVGHGDLKSA TWWFKMQNRK ELIEACSILI WIASALHAAV
NFGQYPYGGY ILNRPTKSRK FMPEKGTPEY DDLAKNYEKA YLRTITPKND TLTDLTIIEV
LSRHASDEQY LGERIEGDDW TTDSVPKEAF KRFGKKLAEI EEKLTQRNND ESLRNRYGPV
KMPYTLLYPS SEEGLTCRGI PNSISI
