ID A0A444XL87_ARAHY Unreviewed; 753 AA.
AC A0A444XL87;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=Ahy_B09g096557 {ECO:0000313|EMBL:RYQ90467.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ90467.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ90467.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYQ90467.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) 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:RYQ90467.1}.
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DR EMBL; SDMP01000019; RYQ90467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444XL87; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000289738; Chromosome b09.
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; 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:SF129; LIPOXYGENASE; 1.
DR Pfam; PF00305; Lipoxygenase; 2.
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:UP000289738}.
FT DOMAIN 1..80
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 83..753
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 132..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 86264 MW; 72EC2D6CF587450E CRC64;
MIKNFIFYAI VFLPGSNTFD WDNEEIGTPG AFLIRNNHHS EFYLKSLTLE DVPSHGVIHF
PCNSWVYPAS KYQNDRVFFS NKTYLPAETP ISLLKYREEE LENLRGDGKG QLQEWDRVYD
YEVYNDLGNP DKGPQHARPV LGGSTEYPYP RRGRTGRAPE YESRLNLALS LNIYVPRDER
FGHLKLADFL SYALKSIVQV LKPEFESIFD KTPNEFDSFE DVLKLYEGGL EVPEGVVKVI
RDNVPLEMLK EIFRTDDEEF AREMLAGINP VMIRSLEEFP PASKLDPKVY GDQTSTITKE
HIESNLEGHT INEVIIERKL FILDHHDALM PYLRRINSTS TKTYASRTLL FLQKNGTLKP
LAIELSLPHP EGDQHGAISK VFVPEEKGVE NSLWQLAKGY VGVVDSGYHQ LISHWLHTHA
VIEPFIIATN RQLSVLHPIY KLLHPHYRDT MNINALGRQI LINAGGALEV TVFTSKYSME
FSSMLYKDWV FPEQALPQDL LKRGVAVKDS SCPHGLKLLI EDYPFAVDGL EIWFAIKTWV
QDYCSVYYKD DESIKKDAEL QSWWKELREK GHGDKKEEIW WPKMQTREEL IETCTIIIWI
ASALHAAINF GQYPYGGYPP NRPAISSKLV PEKGTPEYDE LLANPDKTYL KTFTSQFKAV
LGISLVEILS RHSSDEVYLG QRDTENWTSD AEALEAFAKF GKKIEDIEEG MKRMNNDEKL
RNRYGPVKMP YTLLYPSSEG GLTGRGIPNS VSI
//
