ID A0A1U7WZK3_NICSY Unreviewed; 849 AA.
AC A0A1U7WZK3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=LOC104228802 {ECO:0000313|RefSeq:XP_009779645.1};
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009779645.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|RefSeq:XP_009779645.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009779645.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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}.
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DR RefSeq; XP_009779645.1; XM_009781343.1.
DR AlphaFoldDB; A0A1U7WZK3; -.
DR STRING; 4096.A0A1U7WZK3; -.
DR GeneID; 104228802; -.
DR KEGG; nsy:104228802; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR OrthoDB; 999249at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000189701; Unplaced.
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; 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:SF111; LIPOXYGENASE; 1.
DR Pfam; PF00305; Lipoxygenase; 3.
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; 2.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 3: Inferred from homology;
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:UP000189701}.
FT DOMAIN 18..149
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 152..849
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 216..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 95819 MW; B9CA13D51CE3D78B CRC64;
MASTDKREIK MINGTVLLMK KTPLDLGSSQ LLAPHETYEI LGHKVILQLV SSVHGDQGKT
LKGELGNPSH LRDENKSGSE SKFCVIFEWD HEVLGAPGAF IIKNLNTSEF YLKSLTLEAS
DPSQDTVQFV CNSWVYPAEK YKSDRIFFVN QAWLPSETPA ALRVYREEEL LLLRGNGTGK
LQEWDRVYDY DCYNDLGDPD NGPLYARPVL GGSVEYPYPR RGRTGRPPSK ADPNSESRLP
QIASFAIYVP RDEKFSPLKM TDVLSNSQKA IAQVFAPQLA SLGNLSLNEF NSFDDVLKVY
EPGTPGFLKY PTPHVIREEK SAWMSDEEFG RETLAGLNPV CITGLKEFPL TSKLDPKTFG
DQTSKITREQ IQNQLDGMTI EQAMEVNRLF MLNYHDIVMP YARKVNTSHS KIYASRTVLF
LQKDGTLKPL AIELSLPHPD GDQLGAISKV FTPAENGVEG ALWQIAKAFV AINDSGVHQL
LSHWYFKLTE VYAVYSVTEY LFDHTSNVLH RLRTHASVEP FVIAANRQLS VLHPVYKLLH
PHFRDTMHIN ALARQAVLNA GGIVEKTVFP GPLSMELTSI AYRDWVFPDQ ALPAELVKRG
VAVEDPSSKH GVRLLIEDYP YAVDGLEIWS AIKSWVQEYI CLYYKSDDML QVDTELQAWW
KELREVGHGD KKDEPWWPKM QTRQELIDSV TIIIWMASAL HAAVNFGQYP YGGFAPNRPG
MSRRLIPEPG TPEYEELKVN PVKGYLKTIT PQFQTLIGIS ALEVLSTHTS DEIYLGQRDS
AEWTKDKEAL QAFERFGKKL AEIEENITKM NNDKKWKNRT GPVKMPYTLL YPTSEPGLTA
KGIPNSISI
//
