ID A0A314U9Q9_PRUYE Unreviewed; 845 AA.
AC A0A314U9Q9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=Pyn_12846 {ECO:0000313|EMBL:PQM34147.1};
OS Prunus yedoensis var. nudiflora.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=2094558 {ECO:0000313|EMBL:PQM34147.1, ECO:0000313|Proteomes:UP000250321};
RN [1] {ECO:0000313|EMBL:PQM34147.1, ECO:0000313|Proteomes:UP000250321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jeju island {ECO:0000313|Proteomes:UP000250321};
RC TISSUE=Leaf {ECO:0000313|EMBL:PQM34147.1};
RA Baek S., Kim J.-H., Choi K., Kim G.-B., Cho A., Jang H., Shin C.-H.,
RA Yu H.-J., Mun J.-H.;
RT "Draft genome of wild Prunus yedoensis var. nudiflora.";
RL Submitted (FEB-2018) 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:PQM34147.1}.
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DR EMBL; PJQY01003830; PQM34147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A314U9Q9; -.
DR STRING; 2094558.A0A314U9Q9; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000250321; 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 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; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR PANTHER; PTHR11771:SF133; 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:UP000250321}.
FT DOMAIN 88..220
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 223..845
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 285..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 96293 MW; EB514CBF2A88FCBA CRC64;
MISSFNSNHI NSKALNCIPW NTPNISSPPP NLFSSTKRRR LQQIRKKKAR DQATGGDMVS
TLISSTAVDQ TVQLTALVSV RKSLKLSIQD MMLHWFGNHD HFTHHKEKEK SLVLQLVSTE
TEAESMKPKL SNEAILDWSK DLNLNLINLI NLILGAEKSS YEVKFEVDPK FGMPGAITVS
NKYEKELYLD SINIEGVVHI ACNSWIQPDK DSSEKRIFFS TKAYLPDETP AGLKELREME
LRQLRGDGTG LRLPSDRIYD YDTYNDIGNP DEGIEYVRST LGGNYTHPHP RRCRTGRPPT
STDDNMESPE NEYKRIYVPR DEEFEEAKQG ALDVGNLKGI LRHIIPTLRT IASRDSNVFK
GYADINCLYG TDKSLPKILN KVQEFLKFDP PKLIAGLTSC CLPDEEFGRQ AIAGINPMSI
QRLTVFPPVS KLDPSTYGPQ ESALKEEHII GHLNGMSIQQ ALEENKLFIL DCHDIFLPYL
DQINALDDRR AYGTRTIFLP PTNSDSPSKQ KQVLTPPVDA TTNWLWQIGK AHVSSNDACA
HQLIHHWLRT HACMEPFIIA AHRQLSVMHP IYKLLKPHMR YTLKINALAR QFLINAGGII
ESNFTAGKYC MEMSCAAYRD WWRFDLEGLP ADLLRRGMAV PDSTQVHGIR LVIEDYPYAT
DGLHIWSAIE TLVRTYVNYY YPDATAVNFD TELQTWYNES INLGHADLRH ASWWPKLSTP
DDLTSILATI IWLTSAQHAA LNNGQYPYGG YVPTRSPHMR RLLPEEHDPE YTTFMQDPQK
YFLSSFPSLL EATKYMAVID IISAHSPDEE YIGDRKDLST WSADTVIIEA FYRFSMEMKE
DRKRD
//
