LOXB_SOLLC
ID LOXB_SOLLC Reviewed; 859 AA.
AC P38416;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Linoleate 9S-lipoxygenase B;
DE EC=1.13.11.58;
DE AltName: Full=Lipoxygenase B;
GN Name=LOX1.2; Synonyms=LOXB;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Caruso; TISSUE=Pericarp;
RX PubMed=7972514; DOI=10.1104/pp.106.1.109;
RA Ferrie B.J., Beaudoin N., Burkhart W., Bowsher C.G., Rothstein S.J.;
RT "The cloning of two tomato lipoxygenase genes and their differential
RT expression during fruit ripening.";
RL Plant Physiol. 106:109-118(1994).
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. It catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00726};
CC Note=Binds 1 Fe cation per subunit. Iron is tightly bound.
CC {ECO:0000255|PROSITE-ProRule:PRU00726};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Fruit specific.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; U09025; AAA53183.1; -; mRNA.
DR PIR; T06339; T06339.
DR AlphaFoldDB; P38416; -.
DR SMR; P38416; -.
DR STRING; 4081.Solyc01g099190.2.1; -.
DR PaxDb; P38416; -.
DR PRIDE; P38416; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR InParanoid; P38416; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P38416; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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-UniPathway.
DR CDD; cd01751; PLAT_LH2; 1.
DR Gene3D; 4.10.372.10; -; 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; PTHR11771; 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; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 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; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Reference proteome.
FT CHAIN 1..859
FT /note="Linoleate 9S-lipoxygenase B"
FT /id="PRO_0000220706"
FT DOMAIN 34..158
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 161..859
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 213..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 521
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 526
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 711
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 859
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 859 AA; 97122 MW; DAD79B10AE627434 CRC64;
MSLGGIVDAI LGKDDRPKVK GRVILMKKNV LDFINIGASV VDGISDLLGQ KVSIQLISGS
VNYDGLEGKL SNPAYLESWL TDITPITAGE STFSVTFDWD RDEFGVPGAF IIKNLHLNEF
FLKSLTLEDV PNYGKIHFVC NSWVYPAFRY KSDRIFFANQ AYLPSETPQP LRKYRENELV
ALRGDGTGKL EEWDRVYDYA CYNDLGEPDK GEEYARPILG GSSEYPYPRR GRTGREPTKA
DPNCESRNPL PMSLDIYVPR DERFGHVKKS DFLTSSLKSS LQTLLPAFKA LCDNTPNEFN
SFADVLNLYE GGIKLPEGPW LKAITDNISS EILKDILQTD GQGLLKYPTP QVIQGDKTAW
RTDEEFGREM LAGSNPVLIS RLQEFPPKSK LDPTIYGNQN STITTEHVQD KLNGLTVNEA
IKSNRLFILN HHDIVMPLLR KINMSANTKA YASRTLLFLQ DDRTLKPLAI ELSLPHPDGD
QFGTVSKVYT PADQGVEGSI WQFAKAYVAV NDMGIHQLIS HWLNTHAVIE PFVVATNRHL
SVLHPIHKLL HPHFRNTMNI NALARETLTY DGGFETSLFP AKYSMEMSAA AYKDWVFPEQ
ALPADLLKRG VAVEDLSSPH GIRLLILDYP YAVDGLEIWA AIKSWVTEYC KFYYKSDETV
EKDTELQAWW KELREEGHGD KKDEAWWPKL QTRQELRDCC TIIIWIASAL HAALHFGLYS
YAGYLPNRPT LSCNLMPEPG SVEYEELKTN PDKVFLKTFV PQLQSLLEIS IFEVSSRHAS
DEVYLGQRDS IEWTKDKEPL VAFERFGKML SDIENRIMIM NSHKSWKNRS GPVNVPYTLL
FPTSEEGLTG KGIPNSVSI
