LOX1_TANCI
ID LOX1_TANCI Reviewed; 907 AA.
AC R9WTS6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Lipoxygenase 1, chloroplastic {ECO:0000303|PubMed:23893337};
DE Short=TcLOX1 {ECO:0000303|PubMed:23893337};
DE EC=1.13.11.- {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:23893337};
DE AltName: Full=13-hydroperoxylinolenic acid synthase {ECO:0000305|PubMed:23893337};
DE Flags: Precursor;
GN Name=LOX1 {ECO:0000303|PubMed:23893337};
OS Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum
OS cinerariifolium).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Anthemidinae; Tanacetum.
OX NCBI_TaxID=118510;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND PATHWAY.
RX PubMed=23893337; DOI=10.1007/s11745-013-3815-1;
RA Ramirez A.M., Yang T., Bouwmeester H.J., Jongsma M.A.;
RT "A trichome-specific linoleate lipoxygenase expressed during pyrethrin
RT biosynthesis in pyrethrum.";
RL Lipids 48:1005-1015(2013).
RN [2]
RP REVIEW.
RX PubMed=15964038; DOI=10.1016/j.phytochem.2005.05.005;
RA Matsuda K., Kikuta Y., Haba A., Nakayama K., Katsuda Y., Hatanaka A.,
RA Komai K.;
RT "Biosynthesis of pyrethrin I in seedlings of Chrysanthemum
RT cinerariaefolium.";
RL Phytochemistry 66:1529-1535(2005).
RN [3]
RP REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Component of the monoterpenoid pyrethrins biosynthesis;
CC pyrethrins are widely used plant-derived pesticide (PubMed:30468448).
CC Plant lipoxygenases may be involved in a number of diverse aspects of
CC plant physiology including growth and development, pest resistance, and
CC senescence or responses to wounding. Catalyzes the hydroperoxidation of
CC lipids containing a cis,cis-1,4-pentadiene structure (By similarity).
CC Mediates the peroxidation of linolenic acid leading to the production
CC of 13-hydroperoxylinolenic acid (PubMed:23893337).
CC {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:23893337,
CC ECO:0000303|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = 13-hydroperoxy-
CC (9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:60904,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:144034;
CC Evidence={ECO:0000269|PubMed:23893337};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60905;
CC Evidence={ECO:0000269|PubMed:23893337};
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 -!- PATHWAY: Isoprenoid biosynthesis. {ECO:0000269|PubMed:23893337}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Confined to glandular trichomes in flowers, and, at
CC low levels, in leaves. {ECO:0000269|PubMed:23893337}.
CC -!- DEVELOPMENTAL STAGE: In flowers, expressed in early developmental
CC stages and fades out progressively in later stages.
CC {ECO:0000269|PubMed:23893337}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; KC441523; AGO03785.1; -; mRNA.
DR UniPathway; UPA00382; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
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 Chloroplast; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Plastid; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..907
FT /note="Lipoxygenase 1, chloroplastic"
FT /id="PRO_0000447850"
FT DOMAIN 85..209
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 212..907
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 567
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 572
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 758
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 762
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 907
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 907 AA; 102462 MW; A67212204F04A51F CRC64;
MALAKQIMGA SLMDQKTSVF GSNLCLNHVL VNKHRLRLRK TRKNGSMVVA AISEDLVKLX
RVEKEKPVTF KVRAVLTVRN KNKEDFFKDT IFRKIDAITD QIGWNVVIQL FSNDIDPRTR
AAKKSNEAVL KDWSKKSNVK TERVNYTADI MVDSDFGIPG AITISNKHQK EFFLETITIE
GFACGPVHFP CNSWVQSTKD LPNPRIFFTN QPYLPDETPV GLKSLRYQEL KDLRGDGTGV
RKLSDRIYDY DVYNDLGNPD RGNDFVRPTL GGEKIPYPRR CRTGRVPSDT DITAESRVEK
PFPLYVPRDE QFEESKANAF STGRLRAVLH NLLPSMVTSI SKKNDFKGFS QIDSLYSEGV
FLKLGLQDDL LKKLPLPNLV TRLHESSQGG GLLKYDTPKI LSKDKFAWLR DDEFARQTIA
GVNPVSIEKL KVFPPVSQLD PEKHGPQESA LREEHIVGFL DGRTVKQAIE EDKLFIIDYH
DIYLPFLDRI NALDGRKAYA TRTIFYLNPS GTLKPVAIEL SLPQALPGSE SKRVLTPPSD
ATSNWMWQLA KAHXCSNDAG AHQLVHHFLR THAAIEPFIL AAHRQLSAMH PIYKLLDPHM
RYTLEINQLA RQNLINADGV IEACFTPGRY GMEISASAYK NWRFDLEGLP ADLIRRGMAV
PDPSKPHGLK LVMEDYPYAS DGLMIWEAIQ NWVKTYVNHY YPDSAQVCND RELQAWYAES
INVGHADLRH KDWWPTLAGA DDLTSVLTTI IWLASAQHAA LNFGQYPYGG YIPNRPPLMR
RLLPDVNDPE YLSFHDDPQK YFLSALPSLL QSTKYMAVVD TLSTHSPDEE YIGERQQTDT
WSGDAEIVEA FYAFSAEIQR IEKEIEKRNS DTSLKNRCGA GVLPYELLAP SSGPGATCRG
VPNSISI
