ID A0A3L6RUS7_PANMI Unreviewed; 845 AA.
AC A0A3L6RUS7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=C2845_PM11G18400 {ECO:0000313|EMBL:RLN09190.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN09190.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
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}.
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:RLN09190.1}.
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DR EMBL; PQIB02000007; RLN09190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6RUS7; -.
DR STRING; 4540.A0A3L6RUS7; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000275267; Chromosome 11.
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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000275267}.
FT DOMAIN 21..145
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 148..845
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
SQ SEQUENCE 845 AA; 95801 MW; 246CDC6E8C7D2675 CRC64;
MPFCWDRCPA PAPENHIAIN GTVVVSCHFG LSVPGKTTTL RLYSSTQIDH NTGKGRLSVE
APLRGGKKTK HGPGKTSTMT YQVTLFVDIE FGTPGAIVVK NGLKNDQFFL RYVHLELAED
RSIHFECNSW VYPYKKTNSD RVFFINTSYL PDKTPEALQL LREEELRSLR GNGRGERKDW
ERIYDYDYYN DLGNPDKEDH IRPVLGGTAT YPYPRRCRTG RALFKKDGMT ETRKHMINLD
FYIPPDERFN PTKLAEVLTL AVQAVTHFVI PESRALSQGN INSFKSFDQL RRDMYSKPQQ
PVVEGVVMDK LKTSVPSHKT YKQVSKMVKE TPVKFPIPQV IEDDQEAWRT DEEFAREMLA
GLNPVVIKRL DVFPPVSSGG KKSSITAAHI EGQLEGRTVE KAIEQNRLFI LDHHDYLMPY
LRRINMLGVC IYASRTLLFL KDDSTLKPVL IELSLPSDGG GDDEISRIFL PASDGIDAHL
WQLAKAHVSV NDSGYHQLIS HWLFTHATVE PFIIATKRQL SAMHPVNKLL EPHFKDNMQI
NTLARSILLS AGGILERTMY PGKYAMEMSS AIYSEWRFTE QSLPNELIKR GVASKDPSGG
VTLHIEDYPY AVDGLDVWRA IEGWVQSYCA HFYHSDTAVV GDKELQAWWD DVRLVGHGDR
QHDPACWLKL DTVAHLAETL STLIWIASAL HAAVNFGQYG YAGFMPNRPT RCRRFVPLPG
SPEMVQLETD PEKFFLEMVP NRFTTTLGLA LIEVLSNHTS DELYLGQRAT SSWTDDGEVL
QLLDRFREEL RRVEKRVAER NRDPRLKNRR GPAKVPYMLL FPDVGNIGGK EKGITGKGIP
NSVSI
//
