ID A0A0D3G5R6_9ORYZ Unreviewed; 759 AA.
AC A0A0D3G5R6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART05G10840.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART05G10840.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART05G10840.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART05G10840.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) 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 -!- 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 AlphaFoldDB; A0A0D3G5R6; -.
DR STRING; 65489.A0A0D3G5R6; -.
DR PaxDb; 65489-OBART05G10840-1; -.
DR EnsemblPlants; OBART05G10840.1; OBART05G10840.1; OBART05G10840.
DR Gramene; OBART05G10840.1; OBART05G10840.1; OBART05G10840.
DR eggNOG; ENOG502QU8Q; Eukaryota.
DR HOGENOM; CLU_004282_0_1_1; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000026960; Chromosome 5.
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:SF91; 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; 2.
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:UP000026960}.
FT DOMAIN 21..147
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 150..653
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT DOMAIN 654..759
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
SQ SEQUENCE 759 AA; 85594 MW; AE2CC34A0F4A6011 CRC64;
MPFCPKLWSS AAPAPAQPGS VVINGTVVVA NHFGLSAPGK STTLRLFSGT EVDHETRKGR
LSAEAALRGG KKTRHGKAST TTYQVTFFVD GEFGTPGAVA VKNGNRNDQF FLRHVRLDLA
EDRSIHFDCN SWVYPYKKTT SDRVFFINTS YLPDKTPEAL RLLREEELRS LRGNGRGERK
DWERIYDFDY YNDLGNPDND DHVRPVLGGT KTHPYPRRCR TGRPLSKTDG VTETRKHKLI
NLDYYIPPDE RFSPGKLAEV LAMGVQAVTH FVIPEARSIF HGDVVNFKST EQLRADLYGK
PPQPAADARV MDELKSSVPS HKTYKQVSRI VKDNPAKFPT PQVIHYDTEA WRSDEEFARE
MLAGLNPVVI KRLEVFPPNK SKITTDDIMT QIGGLTIQQA MEQKRMYILD HHDYLMPYLR
RINTEGVCVY ASRTLLFLRD DGALRPVAIE LSLPDGGVGG GEISRVFLPA SQGTDAHLWH
LAKTHVAVND SGYHQLISHW LFTHATVEPF IIATRRQLSA MHPIHKLLDP HFKDNMQINT
LARSILLNAG GLLEKIMYPG KYSMEMSSDI YAHWRFTEQS LPNDLIKRGM ASRDPKARGG
VSLHIEDYPY AVDGIDVWLA IEGWVRSYCD HFYHADAAVA GDAELQAWWD DTVPDRFTAT
LGIALIEVLS NHTSDEVYLG QRATSTWTDD GEVLLLLDRF RDELRRVEKR VEERNKDPRL
VNRRGPVRVP YTLLYPDAGD VAGKEKGITG RGIPNSVSI
//
