ID I1GNI3_BRADI Unreviewed; 864 AA.
AC I1GNI3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=100831787 {ECO:0000313|EnsemblPlants:KQK13306};
GN ORFNames=BRADI_1g09260v3 {ECO:0000313|EMBL:KQK13306.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK13306.1};
RN [1] {ECO:0000313|EMBL:KQK13306.1, ECO:0000313|EnsemblPlants:KQK13306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK13306.1,
RC ECO:0000313|EnsemblPlants:KQK13306};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQK13306.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK13306.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK13306}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK13306};
RG EnsemblPlants;
RL Submitted (AUG-2018) 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 -!- 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 -!- 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}.
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DR EMBL; CM000880; KQK13306.1; -; Genomic_DNA.
DR RefSeq; XP_003559938.1; XM_003559890.3.
DR AlphaFoldDB; I1GNI3; -.
DR STRING; 15368.I1GNI3; -.
DR EnsemblPlants; KQK13306; KQK13306; BRADI_1g09260v3.
DR GeneID; 100831787; -.
DR Gramene; KQK13306; KQK13306; BRADI_1g09260v3.
DR KEGG; bdi:100831787; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; I1GNI3; -.
DR OMA; GQRENPH; -.
DR OrthoDB; 462210at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000008810; Chromosome 1.
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; 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; LIPOXYGENASE; 1.
DR PANTHER; PTHR11771:SF160; 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 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:UP000008810}.
FT DOMAIN 36..163
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 166..864
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
SQ SEQUENCE 864 AA; 96827 MW; DDB39B821C8D5A95 CRC64;
MFGGGLNVLG DLTGGLKNGR LKGSVVLMRK NVLEFNDFSA SLVDGITEFL GRGVTCQLIS
STVVDPNNGN RGKVGAEASL EQWNMARLPF ITAGETKFGV TFDWAVEKMG VPGAIIVKNN
HASEFFLKTI TLDNVPGHGT VVFVANSWVY PQGMYRYNRV FFSNDTYLPS KMPVALKPYR
EDELQNLRGD DQQGPYEEHD RVYRYDVYND LGDNREILGG TKEFPYPRRC RTGRKPSETK
PDHESRLLPV VQNIYVPRDE LFGHLKQSDF LGYTIKALVD GIVPAIRTYV DLSPGEFDSF
KDIVKLYEGG LKLPNIPALE EMRKRFPLQL VKDLIPIGGD YILKLPKPQI IKENEKAWMT
DDEFAREMLA GVNPMMIKRV TEFPPKSTLD PSKYGDHTST ITDAHIRNSL EGLTVQQALA
GNKLYIVDQH DNLMPFLVNI NNLDGSYIYA TRTLLFLRGD GTLTPVAIEL SSPLLQGGLT
TPDSTVYTPA STGVEGWVWQ LAKAYVAVND YGWHQLISHW LNTHAVMEPF IIATNRQLSV
IHPVHKLLHP HYRDTMNINA RARGLLINAG GIIEMTVFPR KYAMEMSSVA YKDWNFTQQG
LPEDLIKRGM AVPDASSPHK VRLLLEDYPY AADGLAVWNA IEQWAADYLA IYYPSDAVLQ
GDVELQAWWK EVREVGHGDL KDAPWWPKMQ TVGELVKACA TIIWTGSALH AAVNFGQYPY
AGYHPNKPSA SRRPMPKPGS EEYALLMREP EKVFIRTITN QLQAIIGISL LEILSKHSSD
EIYLGQRDTP EWTSDAKALE AFKRFGSRLE SIESQVVAMN GNPKLKNRVG PAKFPYMLLY
PNTSDRKGDA EGLTARGIPN SISI
//
