ID A0A445DR47_ARAHY Unreviewed; 904 AA.
AC A0A445DR47;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=Ahy_A03g011567 {ECO:0000313|EMBL:RYR65639.1};
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:RYR65639.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR65639.1, 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:RYR65639.1};
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 -!- 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:RU003975}.
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:RYR65639.1}.
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DR EMBL; SDMP01000003; RYR65639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445DR47; -.
DR STRING; 3818.A0A445DR47; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000289738; Chromosome a03.
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; 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; 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; 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};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU003975};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767,
KW ECO:0000256|RuleBase:RU003975};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738}.
FT DOMAIN 100..224
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 236..904
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 282..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 102777 MW; CAF334C132D2D23A CRC64;
MAAGTKSVML ALLDTFPLHV HHNNASPLCQ ERRLMMLSCI SGRTNNIVRA RQKQIAPTVV
AALIESSEKR DLNTTTITKL TADVAVRSGN NNNNNNVFAS NMKTLVNIFR PTVQPHANKG
LVLQLVSSDQ LGPNGKEAKL SEEIVLEWPE NDVVLGGEGS INTYKVEFCV DSDFGVPGAV
AVLNRYDSEF FLDSINIQQL NLHFPCKSWV QPENKIDPHK RIFFFNKNNQ TLTWQVYLPF
ETPIGLKQVR ERDLRQMRGD SRGRRKSCDR IYEYDVYNDL GDPDKGDEYE RPTLGGQNNP
YPTRCRTGRP PTRIDSHAES RPSGSESIYV PRDEELADIK KHDLDRAKLI AIARNIVPAL
LDKMGNEGVL NIHNFIRESR HSHSNLGGTI EELFKFDPPK IFSRGKSHFL EDDEFGRQVL
AGLNPLSIER LKVFPPVSKL DPCKSALKEE HIIDHIDGMS IQQALEDNKL FILDYHDIFL
PFVDRINALD DRKAYATTTI FFLTKMGTLK AIAIQLALPT MDPNTSSKQV LTPPVDTTTK
WLWQLGKAHV CSNDAFVHTY LHHWLRIHAT MEPFIIAAHR QLSVMHPIYK LLHPHMRYTL
KTNATARETL INAGGILETN FSPGKYSMQI TSAAYRDWWQ FDQEGLPTDL IRRGLAVPDE
SQPQGVRLVI EDYPYAADGL LIWSSIEKLV KTYVNHYYKD VDAISSDYEL QSWYKEFINL
GHPDHKNASW WPKLSTPENL ISILTTIIWI VTAQHAVLNF SQYHYGGYVP MRPALMRKLI
PKEGDLDYID FVMDPQRYFE SSLPSLSQAA KFMAVTSIGS AHSPEEEYIG DRNDLCSWLE
EPEIFDAFKQ FSMEIKNIET EIEKRNADKK LRNRCGVGVT PYELLMPWSD QGVTGRGVPN
SVTA
//
