ID Q43440_SOYBN Unreviewed; 859 AA.
AC Q43440;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 22-FEB-2023, entry version 138.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=vlxC {ECO:0000313|EMBL:AAA96817.1};
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:AAA96817.1};
RN [1] {ECO:0000313|EMBL:AAA96817.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:AAA96817.1};
RX PubMed=1822994; DOI=10.1105/tpc.3.9.973;
RA Tranbarger T.J., Franceschi V.R., Hildebrand D.F., Grimes H.D.;
RT "The soybean 94-kilodalton vegetative storage protein is a lipoxygenase
RT that is localized in paraveinal mesophyll cell vacuoles.";
RL Plant Cell 3:973-987(1991).
RN [2] {ECO:0000313|EMBL:AAA96817.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:AAA96817.1};
RX PubMed=7549487; DOI=10.1105/tpc.7.8.1319;
RA Bunker T.W., Koetje D.S., Stephenson L.C., Creelman R.A., Mullet J.E.,
RA Grimes H.D.;
RT "Sink limitation induces the expression of multiple soybean vegetative
RT lipoxygenase mRNAs while the endogenous jasmonic acid level remains low.";
RL Plant Cell 7:1319-1331(1995).
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; U26457; AAA96817.1; -; mRNA.
DR PIR; T06429; T06429.
DR RefSeq; NP_001235189.1; NM_001248260.1.
DR AlphaFoldDB; Q43440; -.
DR SMR; Q43440; -.
DR BindingDB; Q43440; -.
DR ProMEX; Q43440; -.
DR GeneID; 547856; -.
DR KEGG; gmx:547856; -.
DR OrthoDB; 888244at2759; -.
DR UniPathway; UPA00382; -.
DR ExpressionAtlas; Q43440; 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; 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 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; LIPOXYGENASE; 1.
DR PANTHER; PTHR11771:SF115; SEED LINOLEATE 9S-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 2: Evidence at transcript level;
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}.
FT DOMAIN 48..173
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 176..859
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 222..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 96301 MW; 0293F9A407CD7690 CRC64;
MTGGMFGRKG QKIKGTVVLM PKNVLDFNAI TSVGKGSAKD TATDFLGKGL DALGHAVDAL
TAFAGHSISL QLISATQTDG SGKGKVGNEA YLEKHLPTLP TLGARQEAFD INFEWDASFG
IPGAFYIKNF MTDEFFLVSV KLEDIPNHGT INFVCNSWVY NFKSYKKNRI FFVNDTYLPS
ATPGPLVKYR QEELEVLRGD GTGKRRDFDR IYDYDIYNDL GNPDGGDPRP IIGGSSNYPY
PRRVRTGREK TRKDPNSEKP GEIYVPRDEN FGHLKSSDFL TYGIKSLSQN VIPLFKSIIL
NLRVTSSEFD SFDEVRGLFE GGIKLPTNIL SQISPLPVLK EIFRTDGENT LQFPPPHVIR
VSKSGWMTDD EFAREMIAGV NPNVIRRLQE FPPKSTLDPA TYGDQTSTIT KQQLEINLGG
VTVEEAISAH RLFILDYHDA FFPYLTKINS LPIAKAYATR TILFLKDDGS LKPLAIELSK
PATVSKVVLP ATEGVESTIW LLAKAHVIVN DSGYHQLISH WLNTHAVMEP FAIATNRHLS
VLHPIYKLLY PHYKDTININ GLARQSLINA GGIIEQTFLP GKYSIEMSSV VYKNWVFTDQ
ALPADLVKRG LAVEDPSAPH GLRLVIEDYP YAVDGLEIWD AIKTWVHEYV SVYYPTNAAI
QQDTELQAWW KEVVEKGHGD LKDKPWWPKL QTVEDLIQSC SIIIWTASAL HAAVNFGQYP
YGGYIVNRPT LARRFIPEEG TKEYDEMVKD PQKAYLRTIT PKFETLIDIS VIEILSRHAS
DEVYLGQRDN PNWTTDSKAL EAFKKFGNKL AEIEGKITQR NNDPSLKSRH GPVQLPYTLL
HRSSEEGMSF KGIPNSISI
//
