ID I1JRC2_SOYBN Unreviewed; 858 AA.
AC I1JRC2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=100815550 {ECO:0000313|EnsemblPlants:KRH68548};
GN ORFNames=GLYMA_03G237300 {ECO:0000313|EMBL:KRH68548.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH68548};
RN [1] {ECO:0000313|EMBL:KRH68548.1, ECO:0000313|EnsemblPlants:KRH68548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH68548};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH68548.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH68548}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH68548};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH68548.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH68548.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; CM000836; KRH68548.1; -; Genomic_DNA.
DR RefSeq; XP_003521704.2; XM_003521656.3.
DR AlphaFoldDB; I1JRC2; -.
DR SMR; I1JRC2; -.
DR STRING; 3847.I1JRC2; -.
DR PaxDb; 3847-GLYMA03G39730-1; -.
DR EnsemblPlants; KRH68548; KRH68548; GLYMA_03G237300.
DR GeneID; 100815550; -.
DR Gramene; KRH68548; KRH68548; GLYMA_03G237300.
DR KEGG; gmx:100815550; -.
DR eggNOG; ENOG502QVKD; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; I1JRC2; -.
DR OrthoDB; 462210at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000008827; Chromosome 3.
DR ExpressionAtlas; I1JRC2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000008827}.
FT DOMAIN 16..158
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 161..858
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
SQ SEQUENCE 858 AA; 97648 MW; 09BB2766935BB92E CRC64;
MPQNIVNALS TSMHIIRGTV IVTKKNVLDF NDLSASLLDR LHEFVGKRVS LQLISAVQAD
PGNGMKGKLG KPAYLEDWIT TITPLTAGES AFRVAFDWNG DEDIGTPGAF LVRNNHHSEF
YLKSLTLENV PGHGVIHFIC NSWVYPAHKY KTDRIFFSNK TYLPSETPVP LLKYREEELE
NLRGDGKGTL QEWDRVYDYA YYNDLGDPDK GAQYARPVLG GSIEYPYPRR GRTGRPPTKS
DANSESRLNF AMSLDIYVPR DEKFGHLKLS DFLANALKSI AQIVKPELES LFDSIPEEFD
SFEDVFKLYE GGIKVPESIL KNIRDKIPAE MLKEILRTDG ERFLKFPVPQ VIKEDKSAWR
TDEEFAREML AGVNPVIIRC LKEFPPESKL DSKVYGDQTS TIRKKHIESN MDGLTVNEAI
RQKKLFILDH HDALIPYLRR INSTSTKTYA SRTILFLQND GTLKPLVIEL SLPHPEEDQY
GVISKVYTPA EEGVENSIWQ LAKAYVAVND SGYHQLISHW LNTHAVIEPF VIAANRQLSV
LHPIYKLLHP HFRDTMNINA LARQILINGG GIVEATVFPS KYSMEMSSVI YKNWVFPDQA
LPTDLIKRGM AVKDSGCPHG LRLLIEDYPY AVDGLEIWFA IKKWVQDYCS FYYKEDDTVK
KDSELQSWWK ELREEGHGDK KNEPWWPKMQ TREDLIEVCT IIIWVASALH ASTNFGQYPY
AGFLPNRPTI SRRFMPEEGT SEYDELVNNP DKVFLKTITA QLQTLIGISL IEILSRHSSD
ELHLGQRDTP NWTCDVEPLE AFDEFGKKLV EIEERIMALN NDGKHKNRVG PVNMPYTLLF
PSSKAGLTGM GIPNSVAI
//
