ID A0A059B6Q4_EUCGR Unreviewed; 877 AA.
AC A0A059B6Q4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=EUGRSUZ_H04500 {ECO:0000313|EMBL:KCW61803.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW61803.1};
RN [1] {ECO:0000313|EMBL:KCW61803.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW61803.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) 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 -!- 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 EMBL; KK198760; KCW61803.1; -; Genomic_DNA.
DR RefSeq; XP_018716515.1; XM_018860970.1.
DR AlphaFoldDB; A0A059B6Q4; -.
DR STRING; 71139.A0A059B6Q4; -.
DR EnsemblPlants; KCW61803; KCW61803; EUGRSUZ_H04500.
DR Gramene; KCW61803; KCW61803; EUGRSUZ_H04500.
DR eggNOG; ENOG502QVKD; Eukaryota.
DR InParanoid; A0A059B6Q4; -.
DR OMA; GRIMEMN; -.
DR OrthoDB; 1052764at2759; -.
DR UniPathway; UPA00382; -.
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; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
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; 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:SF126; LINOLEATE 9S-LIPOXYGENASE 1; 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; 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}.
FT DOMAIN 50..181
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 184..877
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 99411 MW; 5AD5A853774D84A8 CRC64;
MADATTTKSV ASNENGNKKM RCEAEELEGG RIRGQVVLRK KKATDFTSFA STIVEVGRGL
VDKVTGHELG GKDVSVQFIS AVNADHGNEL QGKLGNPVHL EDPVKTSACS TPGELAFSLT
HHLDREIGVP GAFLIRNNHH SEFFLKTVTL EDVPGHGQIH FVCNSWVYPA HCYAKDRIFF
ANKTYLPSET PAPLNKYREE ELENLRGDGT GERKEWERVY DYAYYNDLSE PQKGPNYVRP
ILGGSTDHPY PRRGRTGRPP TKEDPDVESR LPILQSLSIY VPRDERFSHI KFSDLLAFAV
KSVAHFLIPA AEGQFDRTPR EFDNFQEILK VYEGGIKLQK NQFIESIMES VPSEMLRELL
RTDSDGFLKF PTPQVIKEDK SAWSTDEEFA REMLAGVDPV LICCLQEFPC KSKLNPENNP
DMRVYIEENL SGRTLDEAIK EKKLFILDHY DTLMPFLRGI NTTSTKTYAT RTLLCLKEDG
TLKPLAIELI LPHPDGDEFG EISEVYKPAK DGIEGTLWDL AKAYVSVNDS GYHQLISHWL
KTHAIIEPFI IATNRQLSVL HPIHKLLHPH FRDTMSINGF ARQILISAGG ALEMTVFPAK
FSLEMSCAAY KDWVFPEQAL PADLIKRGMA VEDANSRHGL RLVIEDYPFA VDGLEIWSAI
ETWVRDYCSF YYKNDEMVQE DTELQSWWKE LREVGHGDLK DKPWWPKMQS LDELIQTCTI
IIWVASALHA AINFGQYPFG GYPPNRPAMS RRLIPEEGTP EYEELQTNRE RALLKTITPQ
ILSLLGISLV EILSTHSPDE VYLGQRDTAE WTSDEAPLQA FEKFGKRLEE IEQRITDMNS
DERLRNRAGL VRMPYTLLYP SSEVGLTGKG IPNSISI
//
