LOX5_ARATH
ID LOX5_ARATH Reviewed; 886 AA.
AC Q9LUW0; Q9FNX7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Linoleate 9S-lipoxygenase 5 {ECO:0000303|PubMed:17369372};
DE EC=1.13.11.58 {ECO:0000269|PubMed:18949503};
DE AltName: Full=Lipoxygenase 5 {ECO:0000303|PubMed:17369372};
DE Short=AtLOX5 {ECO:0000303|PubMed:18949503};
GN Name=LOX5 {ECO:0000303|PubMed:17369372};
GN OrderedLocusNames=At3g22400 {ECO:0000312|Araport:AT3G22400};
GN ORFNames=MCB17.13 {ECO:0000312|EMBL:BAB01777.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-886.
RA Kunze S., Fritsche K., Feussner I.;
RT "AtLOX5, the second 9-LOX of Arabidopsis.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17369372; DOI=10.1105/tpc.106.046052;
RA Vellosillo T., Martinez M., Lopez M.A., Vicente J., Cascon T., Dolan L.,
RA Hamberg M., Castresana C.;
RT "Oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate
RT lateral root development and defense responses through a specific signaling
RT cascade.";
RL Plant Cell 19:831-846(2007).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18949503; DOI=10.1007/s11745-008-3245-7;
RA Bannenberg G., Martinez M., Hamberg M., Castresana C.;
RT "Diversity of the enzymatic activity in the lipoxygenase gene family of
RT Arabidopsis thaliana.";
RL Lipids 44:85-95(2009).
RN [6]
RP FUNCTION.
RX PubMed=21481031; DOI=10.1111/j.1365-313x.2011.04608.x;
RA Lopez M.A., Vicente J., Kulasekaran S., Vellosillo T., Martinez M.,
RA Irigoyen M.L., Cascon T., Bannenberg G., Hamberg M., Castresana C.;
RT "Antagonistic role of 9-lipoxygenase-derived oxylipins and ethylene in the
RT control of oxidative stress, lipid peroxidation and plant defence.";
RL Plant J. 67:447-458(2011).
RN [7]
RP INDUCTION BY GREEN PEACH APHID, AND DISRUPTION PHENOTYPE.
RX PubMed=22474183; DOI=10.1105/tpc.111.094110;
RA Nalam V.J., Keeretaweep J., Sarowar S., Shah J.;
RT "Root-derived oxylipins promote green peach aphid performance on
RT Arabidopsis foliage.";
RL Plant Cell 24:1643-1653(2012).
RN [8]
RP FUNCTION, INDUCTION BY FUSARIUM GRAMINEARUM, AND DISRUPTION PHENOTYPE.
RX PubMed=26075826; DOI=10.1094/mpmi-04-15-0096-r;
RA Nalam V.J., Alam S., Keereetaweep J., Venables B., Burdan D., Lee H.,
RA Trick H.N., Sarowar S., Makandar R., Shah J.;
RT "Facilitation of Fusarium graminearum infection by 9-lipoxygenases in
RT Arabidopsis and wheat.";
RL Mol. Plant Microbe Interact. 28:1142-1152(2015).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26417008; DOI=10.1104/pp.15.00992;
RA Marcos R., Izquierdo Y., Vellosillo T., Kulasekaran S., Cascon T.,
RA Hamberg M., Castresana C.;
RT "9-Lipoxygenase-derived oxylipins activate brassinosteroid signaling to
RT promote cell wall-based defense and limit pathogen infection.";
RL Plant Physiol. 169:2324-2334(2015).
RN [10]
RP FUNCTION.
RX PubMed=28371855; DOI=10.1093/pcp/pcx036;
RA Oenel A., Fekete A., Krischke M., Faul S.C., Gresser G., Havaux M.,
RA Mueller M.J., Berger S.;
RT "Enzymatic and non-enzymatic mechanisms contribute to lipid oxidation
RT during seed aging.";
RL Plant Cell Physiol. 58:925-933(2017).
CC -!- FUNCTION: 9S-lipoxygenase that can use linoleic acid or linolenic acid
CC as substrates. Plant lipoxygenases may be involved in a number of
CC diverse aspects of plant physiology including growth and development,
CC pest resistance, and senescence or responses to wounding. Catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure. Function as regulators of root development by controlling
CC the emergence of lateral roots (PubMed:17369372, PubMed:18949503). 9S-
CC lypoxygenase-derived oxylipins may play an antagonistic role to
CC ethylene signaling in the control of responses involving oxidative
CC stress, lipid peroxidation and plant defense (PubMed:21481031). LOX5-
CC derived oxylipins may facilitate performance of green peach aphid
CC (Myzus persicae) on foliage (PubMed:21481031). 9S-lypoxygenase-derived
CC oxylipins are engaged during infection to control the balance between
CC salicylic acid (SA) and jasmonate (JA) signaling to facilitate
CC infection by the fungal pathogen Fusarium graminearum
CC (PubMed:26075826). 9S-lypoxygenase-derived oxylipins activate
CC brassinosteroid signaling to promote cell wall-based defense and limit
CC pathogen infection (PubMed:26417008). Does not seem to contribute to
CC the oxidation of free fatty acids during seed aging (PubMed:28371855).
CC {ECO:0000269|PubMed:17369372, ECO:0000269|PubMed:18949503,
CC ECO:0000269|PubMed:21481031, ECO:0000269|PubMed:26075826,
CC ECO:0000269|PubMed:26417008, ECO:0000269|PubMed:28371855}.
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:18949503};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30292;
CC Evidence={ECO:0000269|PubMed:18949503};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (9S)-hydroperoxy-
CC (10E,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:51248,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:60962;
CC Evidence={ECO:0000269|PubMed:18949503};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51249;
CC Evidence={ECO:0000269|PubMed:18949503};
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 -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:17369372}.
CC -!- DEVELOPMENTAL STAGE: First observed in lateral root primordia (LRP),
CC from the first pericycle divisions. Disappears before root emergence.
CC {ECO:0000269|PubMed:17369372}.
CC -!- INDUCTION: Induced by the green peach aphid (Myzus persicae)
CC (PubMed:22474183). Induced by infection with the fungal pathogen
CC Fusarium graminearum (PubMed:26075826). {ECO:0000269|PubMed:22474183,
CC ECO:0000269|PubMed:26075826}.
CC -!- DISRUPTION PHENOTYPE: Increment in the number of lateral roots, and
CC moderate increase in the length of the primary root (PubMed:17369372).
CC Reduced performance of green peach aphid (Myzus persicae) on foliage
CC (PubMed:22474183). Enhanced disease resistance to the fungal pathogen
CC Fusarium graminearum (PubMed:26075826). The double mutant plants lox1
CC and lox5 exhibit enhanced susceptibility to the bacterial pathogen
CC Pseudomonas syringae pv tomato DC3000 and the biotrophic powdery mildew
CC pathogen Golovinomyces cichoracearum (PubMed:26417008).
CC {ECO:0000269|PubMed:17369372, ECO:0000269|PubMed:22474183,
CC ECO:0000269|PubMed:26075826, ECO:0000269|PubMed:26417008}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01777.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB022215; BAB01777.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76630.1; -; Genomic_DNA.
DR EMBL; AJ302043; CAC19365.1; -; mRNA.
DR RefSeq; NP_188879.2; NM_113137.4.
DR AlphaFoldDB; Q9LUW0; -.
DR SMR; Q9LUW0; -.
DR STRING; 3702.AT3G22400.1; -.
DR SwissLipids; SLP:000001764; -.
DR iPTMnet; Q9LUW0; -.
DR PaxDb; Q9LUW0; -.
DR PRIDE; Q9LUW0; -.
DR ProteomicsDB; 238484; -.
DR EnsemblPlants; AT3G22400.1; AT3G22400.1; AT3G22400.
DR GeneID; 821808; -.
DR Gramene; AT3G22400.1; AT3G22400.1; AT3G22400.
DR KEGG; ath:AT3G22400; -.
DR Araport; AT3G22400; -.
DR TAIR; locus:2087837; AT3G22400.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; Q9LUW0; -.
DR OMA; WWTELRN; -.
DR OrthoDB; 385042at2759; -.
DR PhylomeDB; Q9LUW0; -.
DR BRENDA; 1.13.11.58; 399.
DR UniPathway; UPA00382; -.
DR PRO; PR:Q9LUW0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUW0; baseline and differential.
DR Genevisible; Q9LUW0; AT.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IDA:UniProtKB.
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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010311; P:lateral root formation; IMP:UniProtKB.
DR GO; GO:0034440; P:lipid oxidation; IDA:TAIR.
DR GO; GO:1900366; P:negative regulation of defense response to insect; IMP:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0048364; P:root development; IMP:TAIR.
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 Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Plant defense; Reference proteome; Stress response.
FT CHAIN 1..886
FT /note="Linoleate 9S-lipoxygenase 5"
FT /id="PRO_0000380594"
FT DOMAIN 35..180
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 183..886
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 234..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 542
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 547
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 733
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 737
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 886
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 886 AA; 101060 MW; 0FF118853811E202 CRC64;
MIHTDIAEIL CVKPKTTKKT KTMEEDVKKT TTMKIEGEVV VMKKNLLDFK DVMASLLDRV
NELLGRRVSL HLISSHQPDP ANEKRGRLGK AAHLEKWVTK IKTSVTAEET AFGVTFDWDE
SMGPPAAFVI KNHHHSQFYL KSLTLRGFPD GEGGATAIHF ICNSWIYPNH RYRSDRVFFS
NKAYLPSETP ELIKELREEE LKNLRGNEKG GEFKEWDRVY DYAYYNDLGA PDKGPDSVRP
VLGGSPELPY PRRGKTGRKS TKSDPKSESR LALLNLNIYV PRDERFSHVK FSDFLAYALK
SVTQVLVPEI ASVCDKTINE FDSFEDVFHL YDGSIKLANG HTISKLRDVI PWEMFRELVR
NDGERFLKYP LPDILKESRS AWRTDEEFAR EMLAGLNPVV ISRLQEFPPK SCLDSAKYGN
QHSSIRTEHI ESNMNGLNVQ EALEQNKLYI LDHHDALMPY LTRINSTNTK TYATRTLLLL
QADGTLKPLA IELSLPHAQG ESYGSVSKVF TPAEKGVEGS VWQLAKAYAA VNDSGYHQLI
SHWLQTHAVI EPFIIASNRQ LSVVHPIHKL LHPHFRDTMN INALARHVLI NSDGVLERTV
FPSRYAMEMS SSIYKNWVFT EQALPKDLLK RGVAVEDPNS DNGVKLLIED YPFAVDGLEI
WSAIKTWVTE YCTFYYNNDK TVQTDTEIQS WWTELRTKGH GDKRHESWWP SMQTRDDLIE
TCTIIIWIAS ALHAAVNFGQ YPYAGFLPNR PTVSRRFMPE PGTDEYAELE EDADVAFLKT
ITPQLQTLLG ISIIEILSMH STDEIYLGQR DSPNWTADDE PLEAFKRFGK ELELIENNII
RRNNDKRFKN RTGPVNIPYT LLYPNTTDYT REGGITGKGI PNSVSI
