AOC2_ARATH
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 03-AUG-2022, entry version 131.
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 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 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 (10Z,15Z)-12-oxophytodienoate; 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}.
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DR EMBL; AJ308484; CAC83762.1; -; mRNA.
DR EMBL; AB028607; BAA95764.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77066.1; -; 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 PDBsum; 1Z8K; -.
DR PDBsum; 2BRJ; -.
DR PDBsum; 2DIO; -.
DR PDBsum; 2GIN; -.
DR PDBsum; 2Q4I; -.
DR PDBsum; 4CQ6; -.
DR PDBsum; 4CQ7; -.
DR AlphaFoldDB; Q9LS02; -.
DR SMR; Q9LS02; -.
DR STRING; 3702.AT3G25770.1; -.
DR iPTMnet; Q9LS02; -.
DR PaxDb; Q9LS02; -.
DR PRIDE; Q9LS02; -.
DR ProteomicsDB; 245005; -.
DR DNASU; 822168; -.
DR EnsemblPlants; AT3G25770.1; AT3G25770.1; AT3G25770.
DR GeneID; 822168; -.
DR Gramene; AT3G25770.1; AT3G25770.1; AT3G25770.
DR KEGG; ath:AT3G25770; -.
DR Araport; AT3G25770; -.
DR TAIR; locus:2086009; AT3G25770.
DR eggNOG; ENOG502QPP8; Eukaryota.
DR HOGENOM; CLU_069000_0_0_1; -.
DR InParanoid; Q9LS02; -.
DR OMA; NLSCNQQ; -.
DR OrthoDB; 1284108at2759; -.
DR PhylomeDB; Q9LS02; -.
DR BioCyc; ARA:AT3G25770-MON; -.
DR BioCyc; MetaCyc:AT3G25770-MON; -.
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 Genevisible; Q9LS02; AT.
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:0009695; P:jasmonic acid biosynthetic process; TAS:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR Gene3D; 2.40.480.10; -; 1.
DR InterPro; IPR009410; Allene_ox_cyc.
DR InterPro; IPR044859; Allene_oxi_cyc_Dirigent.
DR InterPro; IPR034871; Allene_oxi_cyc_sf.
DR PANTHER; PTHR31843; PTHR31843; 1.
DR Pfam; PF06351; Allene_ox_cyc; 1.
DR SUPFAM; SSF141493; SSF141493; 1.
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 220..222
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
