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Database: UniProt
Entry: A0A444Y8X9_ARAHY
LinkDB: A0A444Y8X9_ARAHY
Original site: A0A444Y8X9_ARAHY 
ID   A0A444Y8X9_ARAHY        Unreviewed;       863 AA.
AC   A0A444Y8X9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE            EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN   ORFNames=Ahy_B08g094358 {ECO:0000313|EMBL:RYQ98306.1};
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:RYQ98306.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYQ98306.1, 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:RYQ98306.1};
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:RYQ98306.1}.
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DR   EMBL; SDMP01000018; RYQ98306.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A444Y8X9; -.
DR   STRING; 3818.A0A444Y8X9; -.
DR   OrthoDB; 888244at2759; -.
DR   UniPathway; UPA00382; -.
DR   Proteomes; UP000289738; Chromosome b08.
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:SF122; LINOLEATE 9S-LIPOXYGENASE-4; 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:UP000289738}.
FT   DOMAIN          41..169
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          172..863
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
FT   REGION          220..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  97773 MW;  B5AAFEC4EFF8BCB7 CRC64;
     MFSGVTSLVN RGHKIKGTVV LMRKNVLDIN SLTSAQGLIG QGLGFVGSTI DNLTAFLGRS
     VSLHLISATK PDGNGKGKVG KSTFLEGIIS SLPTLGAGQS AFTIHFEWDD GEMGIPGAFY
     IKNFMQTEFF LLTLTLEDIP NHANLKIHFV CNSWIYNAKN YKTDRIFFSN KTYLPSDTPA
     PLVKYREDEL KNLRGDGKGE RKEYDRIYDY DVYNDLGNPD SNEKYARPVL GGSTLPYPRR
     GRTGRPTTNK DPKSEKRSDF VYLPRDEAFG HLKSSDFLTY GLKSVAQDVM PVLTDAFDSN
     ILTLEFDDFA EVDKLYTGGI TLPTNFLSKF SPLPVLKEIL RTDGEQFLKY PPPKVMQVNK
     SAWMTDEEFS RETLAGVNPN VIKSLEEFPP GSKLDSKVYG DHTSTMKKEH LEPNLEGLTV
     EQAIEKKKLF ILDHHDYLIP YLRRINSSKT KAYATRTIFF LKDDGTLKPL AIELSKPHPQ
     GEEHGPVSDV YLPAHEGVEG YIWVLAKAYV VVNDSCYHQL VSHWLNTHAV VEPFVIATNR
     HLNVVHPINK LLSPHYRDTM NINSLARKAL INADGIIEQT FLWGRYALEM SAVLYKDWVF
     LDQALPNDLI KRGVAVKDSS SPHGVHLVIE DYPYASDGLE IWDAIKSWVK EYVFFYYNSD
     DALKQDTELQ EWWKELVEVG HGDKKNETWW PKMETRNELI EASTTLIWIA SALHAAINFG
     QYPYGGYILN RPTLSRRFMP EKGSPEYDEL AKNHEKEFLK TITGKKETLI DLTVIEILSR
     HASDESYLGQ RDDGEFWTCD TEALDAFKRF GKKLAETEQR LMQKNNDGSL KNRSGPAKMP
     YTLLYPSSEE GLTFRGIPNS ISI
//
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