ID A0A022S0K2_ERYGU Unreviewed; 923 AA.
AC A0A022S0K2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=MIMGU_mgv1a000979mg {ECO:0000313|EMBL:EYU46312.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU46312.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU46312.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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; KI630171; EYU46312.1; -; Genomic_DNA.
DR RefSeq; XP_012829959.1; XM_012974505.1.
DR AlphaFoldDB; A0A022S0K2; -.
DR STRING; 4155.A0A022S0K2; -.
DR GeneID; 105951110; -.
DR KEGG; egt:105951110; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR OMA; CRITASQ; -.
DR OrthoDB; 462210at2759; -.
DR PhylomeDB; A0A022S0K2; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
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:SF194; LINOLEATE 13S-LIPOXYGENASE 2-1, CHLOROPLASTIC; 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; 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:UP000030748}.
FT DOMAIN 103..227
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 230..923
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 281..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 103549 MW; AE9ADB1734A58464 CRC64;
MLKHNFHKSH SASCTTVFPV PIAKPFLSGG GNAAAALSLP ISHKNTTTIP TKKSKRISRG
GVIIRRQYSG SSTGVKAVLI AGSEKSTTTV KAVVTVLQTV GGALTHLGLN RGLDDIADVL
GKTLLVELVA AELDPKSGLE KASIKSYARK TGKDDNETYY EASFEIPEDF GEVGAVLIEN
EHHKEMFLKN IVFNGFSTTT TNDSLEVTCN TWIHPKFDNP EKRVFFTNKS YLPSQTPTAL
ERYREKELEI LRGDGQGERK TADRIYDYDV YNDLGDPDSD VDLARPVLGG PDHPYPRRCR
TGRPRTEKDP LSESRSSSVY VPRDEAFSEV KQMTFSAKTV YSVLHALVPS VQTSIIDTDL
GFPHFTAIDT LFNEGYELPD SSTVVSLRNI IPRLVKAVSD TGNSALRFET PEFIDRDKFA
WFRDTEFGRQ TLAGVNPCCI KLVTEWPLKS NLDPEVYGPA ESAITTELVE QEIGGFTTVD
EALKQKKLFI LDYHDVFLPY VNKVRQLKGT TLYGSRTLFY LTPADTLRPL AIELTRPPID
GKPQWKQVFK PTWDATGVWL WRLAKSHVLA HDSGYHQLVS HWLRTHCCTE PYIIATNRQL
SAMHPIYRLL HPHLRYTMEI NALAREALIN ANGIIESSFS PGKYSMELSS VAYDKLWQFN
LEGLPADLIS RGMAVEDPTA PHGLKLTIED YPYANDGLLL WDAIKQWVAD YVAYYYQEPS
LVESDTELQA WWTEIRTVGH GDKKDEPWWP ELKTPDDLIG ILTTIIWVAS GHHAAVNFGQ
FDFGAYFPNR PTIARTQMPT EEPKDEERKQ FMERPDEFLL KCFPSQVQAT VVMAIIDVLS
NHSPDEEYIG EQIQPYWADD RVINAAFERF NGRLMEIEGI IDARNADTNL KNRAGAGVVP
YELLKPYSEA GVTGKGVPNS ISI
//
