ID   LOX6_ARATH              Reviewed;         917 AA.
AC   Q9CAG3; Q0WLL0; Q56WC0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Lipoxygenase 6, chloroplastic {ECO:0000303|Ref.1};
DE            Short=AtLOX6 {ECO:0000303|Ref.1};
DE            EC=1.13.11.12 {ECO:0000269|PubMed:18949503};
DE   Flags: Precursor;
GN   Name=LOX6 {ECO:0000303|Ref.1};
GN   OrderedLocusNames=At1g67560 {ECO:0000312|Araport:AT1G67560};
GN   ORFNames=F12B7.11 {ECO:0000312|EMBL:AAG52309.1};
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 [MRNA].
RA   Behrends V., Kunze S., Feussner I.;
RT   "AtLOX6, the fourth chloroplastic 13-LOX from Arabidopsis thaliana.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 564-917.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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).
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 (By similarity). 13S-lipoxygenase that can use linolenic acid
CC       as substrates. {ECO:0000250|UniProtKB:Q06327, ECO:0000255|PROSITE-
CC       ProRule:PRU00726, ECO:0000269|PubMed:18949503}.
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:18949503};
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:18949503};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-
CC         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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD95111.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ748537; CAG38328.1; -; mRNA.
DR   EMBL; AC011020; AAG52309.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34664.1; -; Genomic_DNA.
DR   EMBL; AY081253; AAL91142.1; -; mRNA.
DR   EMBL; BT010546; AAQ65169.1; -; mRNA.
DR   EMBL; AK222124; BAD95111.1; ALT_INIT; mRNA.
DR   EMBL; AK230188; BAF01997.1; -; mRNA.
DR   PIR; B96699; B96699.
DR   RefSeq; NP_176923.1; NM_105423.3.
DR   AlphaFoldDB; Q9CAG3; -.
DR   SMR; Q9CAG3; -.
DR   STRING; 3702.Q9CAG3; -.
DR   iPTMnet; Q9CAG3; -.
DR   PaxDb; 3702-AT1G67560-1; -.
DR   ProteomicsDB; 238425; -.
DR   EnsemblPlants; AT1G67560.1; AT1G67560.1; AT1G67560.
DR   GeneID; 843077; -.
DR   Gramene; AT1G67560.1; AT1G67560.1; AT1G67560.
DR   KEGG; ath:AT1G67560; -.
DR   Araport; AT1G67560; -.
DR   TAIR; AT1G67560; LOX6.
DR   eggNOG; ENOG502QQSP; Eukaryota.
DR   HOGENOM; CLU_004282_0_0_1; -.
DR   InParanoid; Q9CAG3; -.
DR   OMA; YTQGHDA; -.
DR   OrthoDB; 462210at2759; -.
DR   PhylomeDB; Q9CAG3; -.
DR   BRENDA; 1.13.11.12; 399.
DR   UniPathway; UPA00382; -.
DR   PRO; PR:Q9CAG3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9CAG3; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009695; P:jasmonic acid biosynthetic process; IMP:CACAO.
DR   GO; GO:0034440; P:lipid oxidation; IDA:TAIR.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009611; P:response to wounding; IMP:CACAO.
DR   CDD; cd01751; PLAT_LH2; 1.
DR   Gene3D; 3.10.450.60; -; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 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; LIPOXYGENASE; 1.
DR   PANTHER; PTHR11771:SF153; LIPOXYGENASE DOMAIN-CONTAINING PROTEIN; 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; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   SUPFAM; SSF48484; Lipoxigenase; 1.
DR   PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR   PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR   PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR   PROSITE; PS50095; PLAT; 1.
DR   Genevisible; Q9CAG3; AT.
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; Transit peptide.
FT   TRANSIT         1..40
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..917
FT                   /note="Lipoxygenase 6, chloroplastic"
FT                   /id="PRO_0000380595"
FT   DOMAIN          98..216
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DOMAIN          219..917
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   REGION          46..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          880..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         575
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         580
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         767
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         771
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         917
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ   SEQUENCE   917 AA;  104516 MW;  14405AD036EC3F64 CRC64;
     MFVASPVKTN FNGVSLVKSP AFSALSCRKQ HRVPISRQVR AVISREEKAV DQEDGKKSTN
     KPLINSSQFP WQRSKYTGSK TVTAVVKIRK KIKEKLTERF EHQLELFMKA IGQGMLIQLV
     SEEIDPETGK GRKSLESPVM GLPKAVKDPR YLVFTADFTV PINFGKPGAI LVTNLLSTEI
     CLSEIIIEDS TDTILFPANT WIHSKNDNPQ ARIIFRSQPC LPSETPDGIK ELREKDLVSV
     RGDGKGERKP HERIYDYDVY NDLGDPRKTE RVRPVLGVPE TPYPRRCRTG RPLVSKDPPC
     ESRGKEKEEF YVPRDEVFEE IKRDTFRAGR FKALFHNLVP SIAAALSNLD IPFTCFSDID
     NLYKSNIVLG HTEPKDTGLG GFIGGFMNGI LNVTETLLKY DTPAVIKWDR FAWLRDNEFG
     RQALAGVNPV NIELLKELPI RSNLDPALYG PQESVLTEEI IAREVEHYGT TIEKALEEKR
     LFLVDYHDIL LPFVEKINSI KEDPRKTYAS RTIFFYSKNG ALRPLAIELS LPPTAESENK
     FVYTHGHDAT THWIWKLAKA HVCSNDAGVH QLVNHWLRTH ASMEPYIIAT NRQLSTMHPV
     YKLLHPHMRY TLEINARARK SLINGGGIIE SCFTPGKYAM ELSSAAYKSM WRFDMEGLPA
     DLVRRGMAEE DSSAECGVRL VIDDYPYAAD GLLIWKAIKD LVESYVKHFY SDSKSITSDL
     ELQAWWDEIK NKGHYDKKDE PWWPKLNTTQ DLSQILTNMI WIASGQHAAI NFGQYPFGGY
     VPNRPTLLRK LIPQETDPDY EMFMRNPQYS FLGSLPTQLQ ATKVMAVQET LSTHSPDEEY
     LIELREVQRH WFQDEQVVKY FNKFSEELVK IEKTINERNK DKKLKNRTGA GMPPYELLLP
     TSPHGVTGRG IPNSISI
//