LOX31_SOLTU
ID LOX31_SOLTU Reviewed; 914 AA.
AC O24371;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Linoleate 13S-lipoxygenase 3-1, chloroplastic;
DE EC=1.13.11.12;
DE Flags: Precursor;
GN Name=LOX3.1; Synonyms=LOX-H3;
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, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Leaf;
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 FUNCTION.
RX PubMed=9927708; DOI=10.1073/pnas.96.3.1146;
RA Royo J., Leon J., Vancanneyt G., Albar J.P., Rosahl S., Ortego F.,
RA Castanera P., Sanchez-Serrano J.J.;
RT "Antisense-mediated depletion of a potato lipoxygenase reduces wound
RT induction of proteinase inhibitors and increases weight gain of insect
RT pests.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1146-1151(1999).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION.
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 [5]
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 lipoxygenases 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. Required for the
CC regulation of wound-induced gene expression, but is not involved in the
CC bulk production of jasmonate upon wounding. Catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure. Linolenic acid is the preferred substrate, before linoleic
CC and arachidonic acids. {ECO:0000269|PubMed:8702864,
CC ECO:0000269|PubMed:9927708}.
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: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: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 6.0. {ECO:0000269|PubMed:8702864};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast
CC thylakoid.
CC -!- TISSUE SPECIFICITY: Expressed in roots and leaves. Detected in tubers
CC and flower buds. {ECO:0000269|PubMed:8702864}.
CC -!- INDUCTION: Up-regulated localy and systemically 30 minutes after
CC wounding. Up-regulated by jasmonate and abscisic acid treatment. Not
CC induced by pathogen infection. {ECO:0000269|PubMed:11080289,
CC ECO:0000269|PubMed:17210991, ECO:0000269|PubMed:8702864}.
CC -!- MISCELLANEOUS: Depletion of LOX-H3 by co-suppression-mediated gene
CC silencing leads to higher tuber yield, but has no effect on the number
CC of tubers per plant.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; X96406; CAA65269.1; -; mRNA.
DR PIR; T07065; T07065.
DR RefSeq; NP_001275115.1; NM_001288186.1.
DR AlphaFoldDB; O24371; -.
DR SMR; O24371; -.
DR STRING; 4113.PGSC0003DMT400058933; -.
DR GeneID; 102597498; -.
DR KEGG; sot:102597498; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR InParanoid; O24371; -.
DR OrthoDB; 385042at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; O24371; 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: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..83
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 84..914
FT /note="Linoleate 13S-lipoxygenase 3-1, chloroplastic"
FT /id="PRO_0000412928"
FT DOMAIN 96..218
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 221..914
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 574
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 579
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 765
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 769
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 914
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 914 AA; 103089 MW; 45BBC7D7180390E4 CRC64;
MALAKEIMGI SLLEKSSSFM NSSSMALFNP NNYHKENHLW FNQQFQGRRN LSRRKAFRQS
TMAAISENLI KVVPEKAVRF KVRAVVTVRN KNKEDLKETI VKHLDAFTDK IGRNVTLELI
STDMDPNTKG PKKSNQAVLK DWSKKSNLKT ERVNYTAEFI VDSNFGNPGA ITVTNKHQQE
FFLESITIEG FACGPVHFPC NSWVQPKKDH PGKRIFFSNQ PYLPDETPAG LKSLRERELR
DLRGDGKGVR KLSDRIYDYD IYNDLGNPDK GIDFARPKLG GDDNVPYPRR CRSGRVPTDT
DISAESRVEK PNPTYVPRDE QFEESKMNTF STSRLKAVLH NLIPSLMASI SSNNHDFKGF
SDIDNLYSKG LLLKLGLQDE VLKKLPLPKV VSSIKEGDLL KYDTPKILSK DKFAWLRDDE
FARQAIAGVN PVSIEKLQFF PPVSKLDPEI YGPQESALKE EHILGHLNGM TVQEALDANK
LFIVDHHDVY LPFLDRINAL DGRKAYATRT IFFLSDVGTL KPIAIELSLP QTGPSSRSKR
VVTPPVCATG NWTWQIAKAH VCANDAGVHQ LVNHWLRTHA SLEPFILAAH RQLSAMHPIY
KLLDPHMRYT LEINGLARQS LINADGVIEA CFTPGRYCME ISAAAYKNWR FDLEGLPADL
IRRGMAVPDS TQPHGLKLLI EDYPYAADGL MIWGAIESWV RDYVNHYYPS SAQVCSDREL
QAWYAETINV GHVDLRNEEW WPTLATPEDL ISILTTLIWL ASAQHAALNF GQYPYGGYVP
NRPPLMRRLI PDENDPEYAV FLADPQKYFF SALPSLLQAT KFMAVVDTLS THSPDEEYLG
ERHQPSTWTG DAEIVEAFYK FSAEIGRIEK EIDERNANTK LKNRCGAGVL PYELLAPSSG
PGVTCRGVPN SVSI
