LOX21_SOLTU
ID LOX21_SOLTU Reviewed; 899 AA.
AC O24370;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Linoleate 13S-lipoxygenase 2-1, chloroplastic {ECO:0000303|PubMed:8702864};
DE EC=1.13.11.12 {ECO:0000269|PubMed:11675388, ECO:0000269|PubMed:8702864};
DE AltName: Full=Lipoxygenase 2-1 {ECO:0000303|PubMed:8702864};
DE Flags: Precursor;
GN Name=LOX2.1 {ECO:0000303|PubMed:8702864};
GN Synonyms=LOX-H1 {ECO:0000303|PubMed:11675388, ECO:0000303|PubMed:17210991,
GN ECO:0000303|PubMed:8702864};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, INDUCTION BY WOUNDING; JASMONATE AND ABSCISIC ACID,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=8702864; DOI=10.1074/jbc.271.35.21012;
RA Royo J., Vancanneyt G., Perez A.G., Sanz C., Stormann K., Rosahl S.,
RA Sanchez-Serrano J.J.;
RT "Characterization of three potato lipoxygenases with distinct enzymatic
RT activities and different organ-specific and wound-regulated expression
RT patterns.";
RL J. Biol. Chem. 271:21012-21019(1996).
RN [2]
RP INDUCTION BY PATHOGEN.
RX PubMed=11080289; DOI=10.1104/pp.124.3.1121;
RA Kolomiets M.V., Chen H., Gladon R.J., Braun E.J., Hannapel D.J.;
RT "A leaf lipoxygenase of potato induced specifically by pathogen
RT infection.";
RL Plant Physiol. 124:1121-1130(2000).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11675388; DOI=10.1074/jbc.m107763200;
RA Leon J., Royo J., Vancanneyt G., Sanz C., Silkowski H., Griffiths G.,
RA Sanchez-Serrano J.J.;
RT "Lipoxygenase H1 gene silencing reveals a specific role in supplying fatty
RT acid hydroperoxides for aliphatic aldehyde production.";
RL J. Biol. Chem. 277:416-423(2002).
RN [4]
RP SUBCELLULAR LOCATION, AND INDUCTION BY WOUNDING.
RX PubMed=17210991; DOI=10.1093/jxb/erl230;
RA Farmaki T., Sanmartin M., Jimenez P., Paneque M., Sanz C., Vancanneyt G.,
RA Leon J., Sanchez-Serrano J.J.;
RT "Differential distribution of the lipoxygenase pathway enzymes within
RT potato chloroplasts.";
RL J. Exp. Bot. 58:555-568(2007).
CC -!- FUNCTION: Plant lipoxygenase involved in a number of diverse aspects of
CC plant physiology including growth and development, pest resistance, and
CC senescence. May not be involved in the bulk production of jasmonate
CC upon wounding. Catalyzes the hydroperoxidation of lipids containing a
CC cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred
CC substrate, before linoleic and arachidonic acids. Has also some
CC activity with phosphatidylglycerol, but not with galactolipids.
CC {ECO:0000269|PubMed:11675388, ECO:0000269|PubMed:8702864}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-
CC octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12;
CC Evidence={ECO:0000269|PubMed:11675388, ECO:0000269|PubMed:8702864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22781;
CC Evidence={ECO:0000269|PubMed:8702864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13S)-hydroperoxy-
CC (9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:34495,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:58757;
CC EC=1.13.11.12; Evidence={ECO:0000269|PubMed:11675388,
CC ECO:0000269|PubMed:8702864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34496;
CC Evidence={ECO:0000269|PubMed:8702864};
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. {ECO:0000255|PROSITE-
CC ProRule:PRU00726};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:8702864};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726, ECO:0000269|PubMed:11675388,
CC ECO:0000269|PubMed:8702864}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P08170}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:11675388, ECO:0000269|PubMed:17210991}. Plastid,
CC chloroplast thylakoid {ECO:0000269|PubMed:17210991}. Note=Associated
CC with the non-appressed part of the thylakoid membrane.
CC {ECO:0000269|PubMed:17210991}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and floral buds.
CC {ECO:0000269|PubMed:8702864}.
CC -!- INDUCTION: Up-regulated by jasmonate and abscisic acid treatment. Up-
CC regulated localy and systemically at the transcript levels 6 hours
CC after wounding, but the protein levels remain constant. Not induced by
CC pathogen infection. {ECO:0000269|PubMed:11080289,
CC ECO:0000269|PubMed:17210991, ECO:0000269|PubMed:8702864}.
CC -!- MISCELLANEOUS: 99% depletion of LOX-H1 by co-suppression-mediated gene
CC silencing has no effect on the basal or wound-induced levels of
CC jasmonates but results in a marked reduction in the production of
CC volatile aliphatic C6 aldehydes. {ECO:0000269|PubMed:11675388}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; X96405; CAA65268.1; -; mRNA.
DR PIR; T07062; T07062.
DR RefSeq; NP_001274843.1; NM_001287914.1.
DR AlphaFoldDB; O24370; -.
DR SMR; O24370; -.
DR STRING; 4113.PGSC0003DMT400081909; -.
DR PRIDE; O24370; -.
DR GeneID; 102596122; -.
DR KEGG; sot:102596122; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR InParanoid; O24370; -.
DR OrthoDB; 385042at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; O24370; baseline.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009534; C:chloroplast thylakoid; IEA:UniProtKB-SubCell.
DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IDA:CACAO.
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:0010597; P:green leaf volatile biosynthetic process; TAS:AgBase.
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 1: Evidence at protein level;
KW Chloroplast; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Plastid; Reference proteome; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 41..899
FT /note="Linoleate 13S-lipoxygenase 2-1, chloroplastic"
FT /id="PRO_0000412927"
FT DOMAIN 78..200
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 203..899
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 252..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 557
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 562
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 749
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 753
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 899
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 899 AA; 101937 MW; 43E9D512C0E808FF CRC64;
MLKPQLQQSS QSTKALIPSW NTNPLFLASF PINILNKNFR LKKKNNFRVH HNYNGASTTK
AVLSSTEKAT GVKAVVTVQK QVNLNLSRGL DDIGDLLGKS LLLWIVAAEL DHKTGIEKPG
IRAYAHRGRD VDGDTHYEAD FVIPQDFGEV GAILIENEHH KEMYVKNIVI DGFVHGKVEI
TCNSWVHSKF DNPDKRIFFT NKSYLPSQTP SGVSRLREEE LVTLRGDGIG ERKVFERIYD
YDVYNDLGEA DSNNDDAKRP VLGGKELPYP RRCKTGRPRS KKDPLSETRS TFVYVPRDEA
FSEVKSVAFS GNTVYSVLHA VVPALESVVT DPNLGFPHFP AIDSLFNVGV DLPGLGDKKS
GLFNVVPRLI KAISDTRKDV LLFESPQLVQ RDKFSWFRDV EFARQTLAGL NPYSIRLVTE
WPLRSKLDPK VYGPPESEIT KELIEKEIGN YMTVEQAVQQ KKLFILDYHD LLLPYVNKVN
ELKGSMLYGS RTIFFLTPQG TLKPLAIELT RPPVDDKPQW KEVYSPNDWN ATGAWLWKLA
KAHVLSHDSG YHQLVSHWLR THCCTEPYII ASNRQLSAMH PIYRLLHPHF RYTMEINALA
REALINANGV IESSFFPGKY AIELSSIAYG AEWRFDQEAL PQNLISRGLA VEDPNEPHGL
KLAIEDYPFA NDGLVLWDIL KQWVTNYVNH YYPQTNLIES DKELQAWWSE IKNVGHGDKR
DEPWWPELKT PNDLIGIITT IVWVTSGHHA AVNFGQYSYA GYFPNRPTVA RSKMPTEDPT
AEEWEWFMNK PEEALLRCFP SQIQATKVMA ILDVLSNHSP DEEYIGEKIE PYWAEDPVIN
AAFEVFSGKL KELEGIIDAR NNDSKLSNRN GAGVMPYELL KPYSEPGVTG KGVPYSISI
