ID B3TDK9_SOYBN Unreviewed; 856 AA.
AC B3TDK9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=100803358 {ECO:0000313|EnsemblPlants:KRH10051};
GN ORFNames=GLYMA_15G026400 {ECO:0000313|EMBL:KRH10051.1};
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|EMBL:ABX60411.1};
RN [1] {ECO:0000313|EMBL:ABX60411.1}
RP NUCLEOTIDE SEQUENCE.
RA Shin J.H., Kim D., Kim K.D., Van K., Kim M.Y., Lee S.-H.;
RT "Sequence level analysis of the lipoxygenase gene family in soybean.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRH10051.1, ECO:0000313|EnsemblPlants:KRH10051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH10051};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH10051.1};
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 [3] {ECO:0000313|EnsemblPlants:KRH10051}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH10051};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KRH10051.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH10051.1};
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; EU028325; ABX60411.1; -; Genomic_DNA.
DR EMBL; CM000848; KRH10051.1; -; Genomic_DNA.
DR RefSeq; XP_003546741.1; XM_003546693.3.
DR AlphaFoldDB; B3TDK9; -.
DR SMR; B3TDK9; -.
DR STRING; 3847.B3TDK9; -.
DR PaxDb; 3847-GLYMA15G03040-1; -.
DR EnsemblPlants; KRH10051; KRH10051; GLYMA_15G026400.
DR GeneID; 100803358; -.
DR Gramene; KRH10051; KRH10051; GLYMA_15G026400.
DR KEGG; gmx:100803358; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR InParanoid; B3TDK9; -.
DR OrthoDB; 888244at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000008827; Chromosome 15.
DR ExpressionAtlas; B3TDK9; 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:SF122; LINOLEATE 9S-LIPOXYGENASE-4; 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 37..162
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 165..856
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 216..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 856 AA; 96377 MW; DFDDCB40BCB70588 CRC64;
MFGIIGGNKG HKIKGNLVIM RKNVLDINSI TSVKGVIGTG INIIGGVVDT VTALASHISI
QLISATKADG HGKGKVGKAT NLRGQVSLPT LGAGEDAYDV HFEWDSDFGI PGAFYIKNFM
QVEFYLKSLT LEDIPNHGTI HFVCNSWVYN SKSYHSDRIF FANNTYLPSE TPAPLVKYRE
EELKNVRGDG TGERKEWDRI YDYDVYNDLG DPDKGEKYAR PVLGGSALPY PRRGRTGRGK
TRKDPNSEKP SDFVYLPRDE AFGHLKSSDF LVYGIKSVAQ DVLPVLTDAF DGNLLSLEFD
NFAEVRKLYE GGVTLPTNFL SKIAPIPVVK EIFRTDGEQF LKYPPPKVMQ VDKSAWMTDE
EFARETIAGV NPNVIKILEE FPPRSKLDSQ AYGDHTSIIT KQHLEPNLGG LTVEQAIQSK
KLFILDHHDY LIPYLRKINA TTTKTYATRT IFFLKSDGTL TPLAIELSKP HPQGEGYGPV
SEVYVPSSEG VEAYIWLLAK AYVVVNDSCY HQLVSHWLNT HAVVEPFVIA TNRHLSVVHP
IYKLLFPHYR DTMNINSLAR KSLVNADGII EKTFLWGRYS LEMSAVIYKD WVFTDQALPN
DLVKRGVAVK DPSAPHGVRL LIEDYPYASD GLEIWDAIKS WVHEYVSFYY KSDAAIQQDP
ELQAWWKELV QVGHGDLKDK PWWQKMQTRE ELIEASATLV WIASALHAAV NFGQYPYGGL
ILNRPTISRR FMPEKGSAEY AALAKNPEKE FLKTITGKKE TLIDLTIIEI LSRHTSDEFY
LGERDGGDYW TSDAGPLEAF KRFGKKLQEI EQKLIQKNKD ETLRNRSGPA KMPYTLLYPS
SEEGLTFRGI PNSISI
//
