LOX2_TANCI
ID LOX2_TANCI Reviewed; 899 AA.
AC R9WS04;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Lipoxygenase 2, chloroplastic {ECO:0000303|PubMed:23893337};
DE Short=TcLOX2 {ECO:0000303|PubMed:23893337};
DE EC=1.13.11.- {ECO:0000255|PROSITE-ProRule:PRU00726};
DE Flags: Precursor;
GN Name=LOX2 {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], AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Plant lipoxygenases 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. Catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure. {ECO:0000255|PROSITE-ProRule:PRU00726}.
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: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Confined to glandular trichomes in flowers.
CC {ECO:0000269|PubMed:23893337}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; KC441524; AGO03786.1; -; 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: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 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..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..899
FT /note="Lipoxygenase 2, chloroplastic"
FT /id="PRO_0000447851"
FT DOMAIN 83..203
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 206..899
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 252..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 557
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 562
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 749
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 753
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 899
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT UNSURE 448
FT /note="E or Q"
FT /evidence="ECO:0000312|EMBL:AGO03786.1"
SQ SEQUENCE 899 AA; 102296 MW; DED757F2B4EE90B1 CRC64;
MLKPQIHKPH LVNKLPLGTP FIPSHASIAS FSTTSLRTLS VQKCYRRYIR YTSSNIKAIM
PDSIGKSIRK KCVVTVQPTI SGALTAVTVG LLGTVADSVS DFLGRSFLLE LVSSDLDSSG
KEKDTVKAYA TYDELDKESK LYKYQCEFEV PDDFGEIGAV LVQNERHRDA YVKNIVLDEI
VTFTCDSWIH SKFDNPDKRI FFLNKSYLPS ETPEGLKSLR QKDLESLRGN GEGERQSFDR
IYDYDTYNDI GDPDTDSDMA RPVLGGNEHP FPRRCRTGRK MTSTEPWSES RTTLPFYVPR
DEDFAEIKQI TRGATTLYSV LHGVIPALSS VLKDEDKGFP LFRDIELLYE KGVDIDPPPD
SGTLSALPRL VKAITNSTKK VLQFETPRIK HKDSFSWFRD EEFCRQTLAG LNPYSIQLVT
EWPLMSKLDP EVYGPAESAI TKETVEEEIK GFMTXEEALE QKRLFLLDYH DLLLPYVNKV
REIEGTTLYG SRTLMFLTCT GTLRPLAIEL TRPPNNGKPQ WKHVYTPCWD ATDXWLWKLA
KAHVLAHDSG YHQLVSHWLR THCVTEPYII ATNRQLSKMH PIQRLLCPHL RYTMQINGLA
RLSLINANGI IESSFSPRKY SMQLSSDAYA QKWRFDHEAL PADLISRGMA VEDESAPHGI
KLTIEDYPFA NDGLLLWDAI KQWATAYINH YYPQAKLVES DEELQAWWTE IRTVGHADKK
DEPWWPQLKT QQDLIGVVST IMWVSSGHHS AVNFGQYDFG GYFPNRPTIA RTKMPNEDPT
FEEWEAFMEK PEDVLLNCFP TQIQATKVMA ILDVLSSHSP DEEYIGTSME ASWEAEPAIK
SAFEEFCGRL KKLDDIIDSR NRDPILRNRT GAGLVQYQLL KPFSGHGVTG KGVPYSISI
