ID A0A0D9X9L8_9ORYZ Unreviewed; 932 AA.
AC A0A0D9X9L8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Lipoxygenase {ECO:0008006|Google:ProtNLM};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR08G16910.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR08G16910.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR08G16910.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR08G16910.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962,
CC ECO:0000256|RuleBase:RU003974};
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}.
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DR AlphaFoldDB; A0A0D9X9L8; -.
DR STRING; 77586.A0A0D9X9L8; -.
DR EnsemblPlants; LPERR08G16910.1; LPERR08G16910.1; LPERR08G16910.
DR Gramene; LPERR08G16910.1; LPERR08G16910.1; LPERR08G16910.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR Proteomes; UP000032180; Chromosome 8.
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:0034440; P:lipid oxidation; IEA:InterPro.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
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; 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; LIPOXYGENASE; 1.
DR PANTHER; PTHR11771:SF127; LIPOXYGENASE 7, CHLOROPLASTIC; 1.
DR Pfam; PF00305; Lipoxygenase; 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; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
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 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 Reference proteome {ECO:0000313|Proteomes:UP000032180}.
FT DOMAIN 95..215
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 222..932
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 268..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 103116 MW; 5BD666F0FAF13DD1 CRC64;
MLPSQLTPST TSSSSGQLYF PSSSCTTLRR PSSSLIAGGR IRQKVVVRCA SSSSSAAAAS
RGGGGRKDSA AAEGSNMAAV KVKAVATFRE TVGGVIRSLR PSKAIDDIKK LVGRSLFLEL
VSSDLDKTGK KKATVQSYAH EVEDEEHGVL TYTAEFDVPA GFGPIGAIVV TNHLRQEMLL
EEVNLTSGNS TPQSIRCKSW VQPKSGEDEG TPGKRVFFAN KTYLPSQTPA GLKSYRNKGL
LEKRGDGISQ READDCVYDY DFYNDLGDAD NSEKDMARPV LGGSKQFPYP RRCRTGRPRS
KKDPKSETRS GTVYVPRDED FSEAKNTQFV LKTARSVLHA AVPVVQSGVQ SDAPVVKSGI
VQPNTTVSFP SFFVIDRLFE NGVELPGLEK ISFLQSILPR LLGAVRDGPG DDILLFDTPA
SVKKDKFAWL RDEEFARETL AGVNPYAIEL VREFPMKSKL DPAVYGPAES AITADVLEAQ
MGHVMTVAEA LKQKRLFMLD YHDLFLPYVH KIRAQKNTTM YGSRTVFFLT DDGTLRLLAI
ELTRPASPSQ PQWRQVFTPS TETTKSWLWR MAKAHVRAHD AGHHELITHW LRTHCAVEPY
IIAANRQLSE MHPIYHLLRP HFRYTMKINA LARTALINAG GIIEQSFSPQ KYSMELSSVA
YDKLWRFDTE ALPADLVRRG MAEEDPTSKH GLKLAINDYP FANDGLLIWD AIKTWVEAYV
ARFYPDNGTV IGDEELQAFW NEVRTVGHGD KKDEPWWPVL DTPASLAHTL TTIIWVAAAH
HAAVNFGQYD FGGYFPNRPS IARTKMPVEE PVDVAAMEKF LDNPDQAIRE CLPSTVQATV
VMAVLDVLST HSSDEEYLSG KETEPWNKDA TVQAAYAAFN ARIKEIEGII DGRNKDKNLK
NRCGAGILPY QLMKPFSDKG VTGMGIPNSI SI
//
