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Database: UniProt
Entry: A0A2P5E723_TREOI
LinkDB: A0A2P5E723_TREOI
Original site: A0A2P5E723_TREOI 
ID   A0A2P5E723_TREOI        Unreviewed;       861 AA.
AC   A0A2P5E723;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   28-JUN-2023, entry version 19.
DE   RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE            EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN   Name=TorLOX10 {ECO:0000313|EMBL:PON81325.1};
GN   ORFNames=TorRG33x02_228530 {ECO:0000313|EMBL:PON81325.1};
OS   Trema orientale (Charcoal tree) (Celtis orientalis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Trema.
OX   NCBI_TaxID=63057 {ECO:0000313|EMBL:PON81325.1, ECO:0000313|Proteomes:UP000237000};
RN   [1] {ECO:0000313|Proteomes:UP000237000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA   Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA   Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA   Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA   Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA   Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA   Smit S., Geurts R.;
RT   "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT   legume Parasponia.";
RL   Submitted (JUN-2016) 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.
CC       {ECO:0000256|RuleBase:RU003975}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962,
CC         ECO:0000256|RuleBase:RU003974};
CC   -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC       {ECO:0000256|RuleBase:RU003975}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family.
CC       {ECO:0000256|ARBA:ARBA00009419, ECO:0000256|RuleBase:RU003974}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PON81325.1}.
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DR   EMBL; JXTC01000219; PON81325.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5E723; -.
DR   STRING; 63057.A0A2P5E723; -.
DR   InParanoid; A0A2P5E723; -.
DR   OrthoDB; 462210at2759; -.
DR   UniPathway; UPA00382; -.
DR   Proteomes; UP000237000; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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:0034440; P:lipid oxidation; IEA:InterPro.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01751; PLAT_LH2; 1.
DR   Gene3D; 3.10.450.60; -; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 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:SF126; LINOLEATE 9S-LIPOXYGENASE 1; 1.
DR   PANTHER; PTHR11771; LIPOXYGENASE; 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; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   SUPFAM; SSF48484; Lipoxigenase; 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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW   ECO:0000256|RuleBase:RU003975};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003974};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU003975};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003974};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003974};
KW   Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767,
KW   ECO:0000256|RuleBase:RU003975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237000}.
FT   DOMAIN          19..161
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          164..861
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
FT   REGION          224..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   861 AA;  98071 MW;  1C72AD39B44118A6 CRC64;
     MFNIINPPSS IFGGGNKKIK GTVVLMKKNL LDFNDIRNGI IDPLNELLGN RVSLQLISAT
     NTDIGNELKG KVGKAAYLEN WTNILTLFPL FAGESAYGVS FEWQEELGVP EAFIIKNNHS
     TEFFLKSLTL EDVPNEGKVH FVCNSWVYPV DKYNYDRVFF RNKTYLPGET PAPLRWYREQ
     ELVNLRGDGT GQRKEGDRVY DYDYYNDLGN PDWGDKFARP VLGGSSEYPY PRRGRTGRPP
     TKTDPNCESR DIDLLNLNFY IPRDERFGHL KMSDFLVNTL KSVALVIKPA LESLFDLTPA
     EFDSFDDVLN LYEGGFPLPL GVFDTIRQNM PIETLKELFR SDGGRFLKFP KPHVIKEDKS
     AWMTDEEFAR EMLAGVNPVL IRRLQEFPPT SKLDPDVYGN QNSTITEEHI NNNLDGLSVN
     EALEKNRLFV LDHHDAFMPY VRRVNTTSSK IYATRTLLFL TNDGTLKPLA IELSLPHPQG
     DHLGAVSRVY TPAEQGVEST IWQLAKAYVT VNDYGYHQLV SHWLNTHAVI EPFVLATNRQ
     LSVLHPIHKL LHPHFRDTMN INALARQVLV NGGGVLESVV FPGKYAMEMS AAVYKNWDLT
     EQSLPADLIK RGVAVKDPSC PHGLRLLIED YPYAVDGLEI WSAIKEWVKD YCSHYYKSDE
     IVQKDKELQS WWKELREVGH GDLKDKPWWP KMHTREELIE TCATVIWITS ALHAAVNFGQ
     YPYAGYLPNR PTISRRLMPE EGTPEYEELR TNPEKAFLRT VTAELQTLVE ISFIEILSKH
     ASDEVYLGQR DSPNWTTDAK PLLAFERFGK KLSEIEDKII SRNNDPTLKN RLGPVKFPYN
     LLIPNGEVGM VAKGIPNSVS I
//
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