LOX12_SOLTU
ID LOX12_SOLTU Reviewed; 861 AA.
AC O24379;
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 9S-lipoxygenase 2;
DE EC=1.13.11.58;
DE AltName: Full=Lipoxygenase 1-2;
GN Name=LOX1.2; Synonyms=LOX1, T8;
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, DEVELOPMENTAL STAGE, INDUCTION BY WOUNDING AND JASMONATE, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Desiree; TISSUE=Tuber;
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).
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 acid is the preferred substrate, but is also active
CC with linolenic and arachidonic acids. {ECO:0000255|PROSITE-
CC ProRule:PRU00726, ECO:0000269|PubMed:8702864}.
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: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. Iron is tightly bound.
CC {ECO:0000255|PROSITE-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: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
CC -!- TISSUE SPECIFICITY: Highly expressed in tubers and roots. Detected in
CC flower buds and leaves. {ECO:0000269|PubMed:8702864}.
CC -!- DEVELOPMENTAL STAGE: Expressed in stolons and increases during early
CC stages of tuber development. {ECO:0000269|PubMed:8702864}.
CC -!- INDUCTION: Up-regulated in roots 2 hours after jasmonate treatment and
CC 24 hours after wounding. Not induced in the leaves.
CC {ECO:0000269|PubMed:8702864}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; X95513; CAA64766.1; -; mRNA.
DR RefSeq; NP_001275357.1; NM_001288428.1.
DR AlphaFoldDB; O24379; -.
DR SMR; O24379; -.
DR PRIDE; O24379; -.
DR GeneID; 102602192; -.
DR KEGG; sot:102602192; -.
DR eggNOG; ENOG502QVKD; Eukaryota.
DR InParanoid; O24379; -.
DR OrthoDB; 385042at2759; -.
DR BioCyc; MetaCyc:MON-12726; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; O24379; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IDA:CACAO.
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..861
FT /note="Linoleate 9S-lipoxygenase 2"
FT /id="PRO_0000412920"
FT DOMAIN 29..160
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 163..861
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 212..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 522
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 527
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 717
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 861
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 861 AA; 97067 MW; 25783F32C69BFA26 CRC64;
MIGQITSGLF GGPDDSKKLK GTVVMMNKNA LDFTDLAGSL TDKAFEFLGQ TVSFQLISSV
QGDPTNGLQG KHSNPAYLEN SLFTLTPLTA GSETAFGVTF DWNEEFGVPG AFIIKNTHIN
EFFLKSLTLE DVPNHGKVHF VCNSWVYPSF RYKSDRIFFV NQPYLPSKTP ELLRKYRENE
LLTLRGDGTG KREAWDRIYD YDIYNDLGNP DEGKENVRTT LGGSAEYPYP RRGRTGRPPT
RTDPKSESRI PLILSLDIYV PRDERFGHLK MSDFLTYALK SIVQFILPEL HALFDGTPNE
FDSFEDVLRL YEGGIKLPQG PLFKALTAAI PLEMIRELLR TDGEGILRFP TPLVIKDSKT
AWRTDEEFAR EMLAGVNPVI ISRLQEFPPK SKLDPEAYGN QNSTITAEHI EDKLDGLTVD
EAMNNNKLFI LNHHDVLIPY LRRINTTTTK TYASRTLLFL QDNGSLKPLA IELSLPHPDG
DQFGVTSKVY TPSDQGVESS IWQLAKAYVA VNDSGVHQLI SHWLNTHAVI EPFVIATNRQ
LSVLHPIHKL LYPHFRDTMN INAMARQILI NAGGVLESTV FQSKFAMEMS AVVYKDWVFP
DQALPADLVK RGVAVEDSSS PHGVRLLIED YPYAVDGLEI WSAIKSWVSD YCSFYYGSDE
EILKDNELQA WWKELREVGH GDKKNEPWWP EMERPQELID SCTTIIWIAS ALHAAVNFGQ
YPYAGYLPNR PTVSRRFMPE PGTPEYEELK KNPDKAFLKT ITAQLQTLLG VSLIEILSRH
TTDEIYLGQR ESPEWTKDKE PLAAFDKFGK KLTDIEKQII QRNGDNILTN RSGPVNAPYT
LLFPTSEGGL TGKGIPNSVS I
