LOX16_SOLTU
ID LOX16_SOLTU Reviewed; 857 AA.
AC Q41238;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Linoleate 9S-lipoxygenase 6;
DE EC=1.13.11.58;
DE AltName: Full=Lipoxygenase 1-5;
DE Short=StLOX1;
DE Short=lox1:St:3;
DE Flags: Fragment;
GN Name=LOX1.6;
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], CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=cv. Desiree;
RX PubMed=8029354; DOI=10.1104/pp.105.1.269;
RA Geerts A., Feltkamp D., Rosahl S.;
RT "Expression of lipoxygenase in wounded tubers of Solanum tuberosum L.";
RL Plant Physiol. 105:269-277(1994).
RN [2]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF VAL-576.
RX PubMed=19037675; DOI=10.1007/s11745-008-3264-4;
RA Andreou A.Z., Hornung E., Kunze S., Rosahl S., Feussner I.;
RT "On the substrate binding of linoleate 9-lipoxygenases.";
RL Lipids 44:207-215(2009).
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. Catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure. Linoleic and linolenic acids are the preferred substrates,
CC but is also active with arachidonic acid. The products are almost
CC exclusively the S enantiomers.
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 Evidence={ECO:0000269|PubMed:19037675, ECO:0000269|PubMed:8029354};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5-7.0. {ECO:0000269|PubMed:8029354};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
CC -!- TISSUE SPECIFICITY: Expressed in tubers and roots. Detected in leaves,
CC petioles and stems.
CC -!- INDUCTION: Up-regulated in stored tubers 8 hours after wounding and by
CC jasmonate. Down-regulated in growing tubers containing already high
CC levels of LOX1.5 at the time of wounding.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; S73865; AAB31252.1; -; mRNA.
DR AlphaFoldDB; Q41238; -.
DR SMR; Q41238; -.
DR PRIDE; Q41238; -.
DR KEGG; ag:AAB31252; -.
DR InParanoid; Q41238; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q41238; 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 1: Evidence at protein 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..857
FT /note="Linoleate 9S-lipoxygenase 6"
FT /id="PRO_0000412924"
FT DOMAIN 26..156
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 159..857
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 205..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 518
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 523
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 709
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 713
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 857
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT MUTAGEN 576
FT /note="V->F: Altered specificity against arachidonic acid."
FT /evidence="ECO:0000269|PubMed:19037675"
FT NON_TER 1
SQ SEQUENCE 857 AA; 96586 MW; 3785A24E8DBA8DA7 CRC64;
QIVGGLIGGH HDSKKVKGTV VMMKKNALDF TDLAGSLTDK IFEALGQKVS FQLISSVQSD
PANGLQGKHS NPAYLENFLF TLTPLAAGET AFGVTFDWNE EFGVPGAFII KNTHINEFFL
KSLTLEDVPN HGKVHFVCNS WVYPSFRYKS DRIFFANQPY LPSETPELLR KYRENELLTL
RGDGTGKREA WDRIYDYDVY NDLGNPDQGE QNVRTTLGGS ADYPYPRRGR TGRPPTRTDP
KSESRIPLIL SLDIYVPRDE RFGHLKMSDF LTYALKSIVQ FILPELHALF DGTPNEFDSF
EDVLRLYEGG IKLPQGPLFK ALTAAIPLEM MKELLRTDGE GILRFPTPLV IKDSKTAWRT
DEEFAREMLA GVNPIIISRL QEFPPKSKLD PEAYGNQNST ITAEHIEDKL DGLTVDEAMN
NNKLFILNHH DVLIPYLRRI NTTTTKTYAS RTLLFLQDNG SLKPLAIELS LPHPDGDQFG
VISKVYTPSD QGVESSIWQL AKAYVAVNDS GVHQLISHWL NTHAVIEPFV IATNRQLSVL
HPIHKLLYPH FRDTMNINAM ARQILINAGG VLESTVFPSK FAMEMSAVVY KDWVFPDQAL
PADLVKRGVA VEDSSSPHGV RLLIEDYPYA VDGLEIWSAI KSWVTDYCSF YYGSDEEILK
DNELQAWWKE LREVGHGDKK NEPWWPEMET PQELIDSCTT IIWIASALHA AVNFGQYPYA
GYLPNRPTVS RRFMPEPGTP EYEELKKNPD KAFLKTITAQ LQTLLGVSLI EILSRHTTDE
IYLGQRESPE WTKDKEPLAA FDKFGKKLTD IEKQIIQRNG DNILTNRSGP VNAPYTLLFP
TSEGGLTGKG IPNSVSI
