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Protein

Lipoxygenase 6, chloroplastic

Gene

LOX6

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure (By similarity). 13S-lipoxygenase that can use linolenic acid as substrates.PROSITE-ProRule annotation1 Publication

Catalytic activityi

Linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate.
Alpha-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate.

Cofactori

Fe cationPROSITE-ProRule annotationNote: Binds 1 Fe cation per subunit.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi575 – 5751Iron; catalyticPROSITE-ProRule annotation
Metal bindingi580 – 5801Iron; catalyticPROSITE-ProRule annotation
Metal bindingi767 – 7671Iron; catalyticPROSITE-ProRule annotation
Metal bindingi771 – 7711Iron; catalyticPROSITE-ProRule annotation
Metal bindingi917 – 9171Iron; via carboxylate; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  • linoleate 13S-lipoxygenase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • jasmonic acid biosynthetic process Source: CACAO
  • lipid oxidation Source: TAIR
  • oxylipin biosynthetic process Source: UniProtKB-UniPathway
  • response to wounding Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Oxylipin biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.12. 399.
ReactomeiREACT_286810. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
REACT_290235. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_302288. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_319433. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_340430. Synthesis of Lipoxins (LX).
UniPathwayiUPA00382.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoxygenase 6, chloroplastic (EC:1.13.11.12)
Short name:
AtLOX6
Gene namesi
Name:LOX6
Ordered Locus Names:At1g67560
ORF Names:F12B7.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G67560.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040ChloroplastSequence AnalysisAdd
BLAST
Chaini41 – 917877Lipoxygenase 6, chloroplasticPRO_0000380595Add
BLAST

Proteomic databases

PaxDbiQ9CAG3.
PRIDEiQ9CAG3.

Expressioni

Gene expression databases

GenevestigatoriQ9CAG3.

Structurei

3D structure databases

ProteinModelPortaliQ9CAG3.
SMRiQ9CAG3. Positions 105-917.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 216119PLATPROSITE-ProRule annotationAdd
BLAST
Domaini219 – 917699LipoxygenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the lipoxygenase family.Curated
Contains 1 lipoxygenase domain.PROSITE-ProRule annotation
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG69653.
HOGENOMiHOG000230469.
InParanoidiQ9CAG3.
KOiK00454.
OMAiNLHGKEF.
PhylomeDBiQ9CAG3.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001246. LipOase_plant.
IPR027433. Lipoxygenase_domain_3.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CAG3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFVASPVKTN FNGVSLVKSP AFSALSCRKQ HRVPISRQVR AVISREEKAV
60 70 80 90 100
DQEDGKKSTN KPLINSSQFP WQRSKYTGSK TVTAVVKIRK KIKEKLTERF
110 120 130 140 150
EHQLELFMKA IGQGMLIQLV SEEIDPETGK GRKSLESPVM GLPKAVKDPR
160 170 180 190 200
YLVFTADFTV PINFGKPGAI LVTNLLSTEI CLSEIIIEDS TDTILFPANT
210 220 230 240 250
WIHSKNDNPQ ARIIFRSQPC LPSETPDGIK ELREKDLVSV RGDGKGERKP
260 270 280 290 300
HERIYDYDVY NDLGDPRKTE RVRPVLGVPE TPYPRRCRTG RPLVSKDPPC
310 320 330 340 350
ESRGKEKEEF YVPRDEVFEE IKRDTFRAGR FKALFHNLVP SIAAALSNLD
360 370 380 390 400
IPFTCFSDID NLYKSNIVLG HTEPKDTGLG GFIGGFMNGI LNVTETLLKY
410 420 430 440 450
DTPAVIKWDR FAWLRDNEFG RQALAGVNPV NIELLKELPI RSNLDPALYG
460 470 480 490 500
PQESVLTEEI IAREVEHYGT TIEKALEEKR LFLVDYHDIL LPFVEKINSI
510 520 530 540 550
KEDPRKTYAS RTIFFYSKNG ALRPLAIELS LPPTAESENK FVYTHGHDAT
560 570 580 590 600
THWIWKLAKA HVCSNDAGVH QLVNHWLRTH ASMEPYIIAT NRQLSTMHPV
610 620 630 640 650
YKLLHPHMRY TLEINARARK SLINGGGIIE SCFTPGKYAM ELSSAAYKSM
660 670 680 690 700
WRFDMEGLPA DLVRRGMAEE DSSAECGVRL VIDDYPYAAD GLLIWKAIKD
710 720 730 740 750
LVESYVKHFY SDSKSITSDL ELQAWWDEIK NKGHYDKKDE PWWPKLNTTQ
760 770 780 790 800
DLSQILTNMI WIASGQHAAI NFGQYPFGGY VPNRPTLLRK LIPQETDPDY
810 820 830 840 850
EMFMRNPQYS FLGSLPTQLQ ATKVMAVQET LSTHSPDEEY LIELREVQRH
860 870 880 890 900
WFQDEQVVKY FNKFSEELVK IEKTINERNK DKKLKNRTGA GMPPYELLLP
910
TSPHGVTGRG IPNSISI
Length:917
Mass (Da):104,516
Last modified:June 1, 2001 - v1
Checksum:i14405AD036EC3F64
GO

Sequence cautioni

The sequence BAD95111.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ748537 mRNA. Translation: CAG38328.1.
AC011020 Genomic DNA. Translation: AAG52309.1.
CP002684 Genomic DNA. Translation: AEE34664.1.
AY081253 mRNA. Translation: AAL91142.1.
BT010546 mRNA. Translation: AAQ65169.1.
AK222124 mRNA. Translation: BAD95111.1. Different initiation.
AK230188 mRNA. Translation: BAF01997.1.
PIRiB96699.
RefSeqiNP_176923.1. NM_105423.2.
UniGeneiAt.27885.

Genome annotation databases

EnsemblPlantsiAT1G67560.1; AT1G67560.1; AT1G67560.
GeneIDi843077.
KEGGiath:AT1G67560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ748537 mRNA. Translation: CAG38328.1.
AC011020 Genomic DNA. Translation: AAG52309.1.
CP002684 Genomic DNA. Translation: AEE34664.1.
AY081253 mRNA. Translation: AAL91142.1.
BT010546 mRNA. Translation: AAQ65169.1.
AK222124 mRNA. Translation: BAD95111.1. Different initiation.
AK230188 mRNA. Translation: BAF01997.1.
PIRiB96699.
RefSeqiNP_176923.1. NM_105423.2.
UniGeneiAt.27885.

3D structure databases

ProteinModelPortaliQ9CAG3.
SMRiQ9CAG3. Positions 105-917.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ9CAG3.
PRIDEiQ9CAG3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G67560.1; AT1G67560.1; AT1G67560.
GeneIDi843077.
KEGGiath:AT1G67560.

Organism-specific databases

TAIRiAT1G67560.

Phylogenomic databases

eggNOGiNOG69653.
HOGENOMiHOG000230469.
InParanoidiQ9CAG3.
KOiK00454.
OMAiNLHGKEF.
PhylomeDBiQ9CAG3.

Enzyme and pathway databases

UniPathwayiUPA00382.
BRENDAi1.13.11.12. 399.
ReactomeiREACT_286810. Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
REACT_290235. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_302288. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_319433. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_340430. Synthesis of Lipoxins (LX).

Miscellaneous databases

PROiQ9CAG3.

Gene expression databases

GenevestigatoriQ9CAG3.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001246. LipOase_plant.
IPR027433. Lipoxygenase_domain_3.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "AtLOX6, the fourth chloroplastic 13-LOX from Arabidopsis thaliana."
    Behrends V., Kunze S., Feussner I.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 564-917.
    Strain: cv. Columbia.
  6. "The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions."
    Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S.
    Curr. Biol. 14:354-362(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Diversity of the enzymatic activity in the lipoxygenase gene family of Arabidopsis thaliana."
    Bannenberg G., Martinez M., Hamberg M., Castresana C.
    Lipids 44:85-95(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiLOX6_ARATH
AccessioniPrimary (citable) accession number: Q9CAG3
Secondary accession number(s): Q0WLL0, Q56WC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 1, 2001
Last modified: April 29, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.