ID   AOC2_ARATH              Reviewed;         253 AA.
AC   Q9LS02;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   02-SEP-2026, entry version 145.
DE   RecName: Full=Allene oxide cyclase 2, chloroplastic;
DE            EC=5.3.99.6;
DE   Flags: Precursor;
GN   Name=AOC2; OrderedLocusNames=At3g25770; ORFNames=K13N2.11, K13N2_9;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RX   PubMed=12777050; DOI=10.1023/a:1023049319723;
RA   Stenzel I., Hause B., Miersch O., Kurz T., Maucher H., Weichart H.,
RA   Ziegler J., Feussner I., Wasternack C.;
RT   "Jasmonate biosynthesis and the allene oxide cyclase family of Arabidopsis
RT   thaliana.";
RL   Plant Mol. Biol. 51:895-911(2003).
RN   [2]
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   [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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 62-253.
RG   Center for eukaryotic structural genomics (CESG);
RT   "X-ray structure of allene oxide cyclase from Arabidopsis thaliana
RT   At3g25770.";
RL   Submitted (APR-2005) to the PDB data bank.
CC   -!- FUNCTION: Involved in the production of 12-oxo-phytodienoic acid
CC       (OPDA), a precursor of jasmonic acid.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate =
CC         (9S,13S,15Z)-12-oxophyto-10,15-dienoate; Xref=Rhea:RHEA:22592,
CC         ChEBI:CHEBI:36438, ChEBI:CHEBI:57411; EC=5.3.99.6;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:12777050}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in fully developed leaves.
CC       {ECO:0000269|PubMed:12777050}.
CC   -!- INDUCTION: High local and systemic induction by wounding.
CC       {ECO:0000269|PubMed:12777050}.
CC   -!- MISCELLANEOUS: The four allene oxide cyclase proteins (AOC1, AOC2, AOC3
CC       and AOC4) are encoded by duplicated genes. They are very similar, and
CC       most experiments involving antibodies do not discriminate between the
CC       different members.
CC   -!- SIMILARITY: Belongs to the allene oxide cyclase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ308484; CAC83762.1; -; mRNA.
DR   EMBL; AB028607; BAA95764.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77066.1; -; Genomic_DNA.
DR   EMBL; OZ408685; CAO7042363.1; -; Genomic_DNA.
DR   EMBL; AY054131; AAL06792.1; -; mRNA.
DR   EMBL; AF380630; AAK55711.1; -; mRNA.
DR   RefSeq; NP_566776.1; NM_113476.4.
DR   PDB; 1Z8K; X-ray; 1.71 A; A/B/C=62-253.
DR   PDB; 2BRJ; X-ray; 1.50 A; A/B/C=78-253.
DR   PDB; 2DIO; X-ray; 1.70 A; A/B/C=78-253.
DR   PDB; 2GIN; X-ray; 1.80 A; A/B/C/D/E/F=78-253.
DR   PDB; 2Q4I; X-ray; 1.71 A; A/B/C=62-253.
DR   PDB; 4CQ6; X-ray; 1.80 A; A/B/C=78-253.
DR   PDB; 4CQ7; X-ray; 1.70 A; A/B/C=78-253.
DR   AlphaFoldDB; Q9LS02; -.
DR   SMR; Q9LS02; -.
DR   FunCoup; Q9LS02; 264.
DR   STRING; 3702.Q9LS02; -.
DR   iPTMnet; Q9LS02; -.
DR   PaxDb; 3702-Q9LS02; -.
DR   ProteomicsDB; 245005; -.
DR   DNASU; 822168; -.
DR   GeneID; 822168; -.
DR   KEGG; ath:AT3G25770; -.
DR   Araport; AT3G25770; -.
DR   TAIR; AT3G25770; AOC2.
DR   eggNOG; ENOG502QPP8; Eukaryota.
DR   HOGENOM; CLU_069000_0_0_1; -.
DR   InParanoid; Q9LS02; -.
DR   OMA; SVQGPYM; -.
DR   PhylomeDB; Q9LS02; -.
DR   BioCyc; ARA:AT3G25770-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G25770-MONOMER; -.
DR   BRENDA; 5.3.99.6; 399.
DR   EvolutionaryTrace; Q9LS02; -.
DR   PRO; PR:Q9LS02; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LS02; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0010319; C:stromule; IDA:TAIR.
DR   GO; GO:0046423; F:allene-oxide cyclase activity; IDA:TAIR.
DR   GO; GO:0009864; P:induced systemic resistance, jasmonic acid mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0009695; P:jasmonic acid biosynthetic process; TAS:TAIR.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   FunFam; 2.40.480.10:FF:000001; Allene oxide cyclase, chloroplastic; 1.
DR   Gene3D; 2.40.480.10; Allene oxide cyclase-like; 1.
DR   InterPro; IPR009410; Allene_ox_cyc.
DR   InterPro; IPR044859; Allene_oxi_cyc_Dirigent.
DR   InterPro; IPR034871; Allene_oxi_cyc_sf.
DR   PANTHER; PTHR31843:SF9; ALLENE OXIDE CYCLASE 1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR31843; ALLENE OXIDE CYCLASE 4, CHLOROPLASTIC; 1.
DR   Pfam; PF06351; Allene_ox_cyc; 1.
DR   SUPFAM; SSF141493; Allene oxide cyclase-like; 1.
DR   PDBsum; 1Z8K; -.
DR   PDBsum; 2BRJ; -.
DR   PDBsum; 2DIO; -.
DR   PDBsum; 2GIN; -.
DR   PDBsum; 2Q4I; -.
DR   PDBsum; 4CQ6; -.
DR   PDBsum; 4CQ7; -.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Isomerase; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..77
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           78..253
FT                   /note="Allene oxide cyclase 2, chloroplastic"
FT                   /id="PRO_0000001703"
FT   STRAND          82..89
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   STRAND          104..108
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   STRAND          113..116
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   STRAND          119..122
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   STRAND          128..142
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   STRAND          147..157
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   STRAND          162..171
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   STRAND          176..185
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   TURN            186..189
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   STRAND          191..200
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   TURN            201..203
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   STRAND          204..212
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   HELIX           217..219
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   HELIX           225..229
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   HELIX           237..240
FT                   /evidence="ECO:0007829|PDB:2BRJ"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:2BRJ"
SQ   SEQUENCE   253 AA;  27635 MW;  1E735E6AF9EBDBAC CRC64;
     MASSAVSLQS ISMTTLNNLS CNQQFHRSSL LGSSKSFQNL GISSNGSDFS YPSSFTAKKN
     LTASRALSQN GNIENPRPSK VQELSVYEIN ELDRHSPKIL KNAFSLMFGL GDLVPFTNKL
     YTGDLKKRVG ITAGLCVVIE HVPEKKGERF EATYSFYFGD YGHLSVQGPY LTYEDSFLAI
     TGGAGIFEGA YGQVKLQQLV YPTKLFYTFY LKGLANDLPL ELTGTPVPPS KDIEPAPEAK
     ALEPSGVISN YTN
//