AOS2_SOLLC
ID AOS2_SOLLC Reviewed; 510 AA.
AC Q9LLB0;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Allene oxide synthase 2, chloroplastic {ECO:0000303|PubMed:12351632};
DE Short=LeAOS2 {ECO:0000303|PubMed:12351632};
DE EC=4.2.1.92 {ECO:0000269|PubMed:10859201};
DE AltName: Full=Cytochrome P450 74A {ECO:0000305};
DE Flags: Precursor;
GN Name=AOS2 {ECO:0000303|PubMed:12351632}; OrderedLocusNames=Solyc11g069800;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND TISSUE SPECIFICITY.
RX PubMed=10859201; DOI=10.1104/pp.123.2.711;
RA Howe G.A., Lee G.I., Itoh A., Li L., DeRocher A.E.;
RT "Cytochrome P450-dependent metabolism of oxylipins in tomato. Cloning and
RT expression of allene oxide synthase and fatty acid hydroperoxide lyase.";
RL Plant Physiol. 123:711-724(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [3]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF CYS-465.
RX PubMed=11154338; DOI=10.1104/pp.125.1.306;
RA Froehlich J.E., Itoh A., Howe G.A.;
RT "Tomato allene oxide synthase and fatty acid hydroperoxide lyase, two
RT cytochrome P450s involved in oxylipin metabolism, are targeted to different
RT membranes of chloroplast envelope.";
RL Plant Physiol. 125:306-317(2001).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12351632; DOI=10.1074/jbc.m207234200;
RA Itoh A., Schilmiller A.L., McCaig B.C., Howe G.A.;
RT "Identification of a jasmonate-regulated allene oxide synthase that
RT metabolizes 9-hydroperoxides of linoleic and linolenic acids.";
RL J. Biol. Chem. 277:46051-46058(2002).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12826630; DOI=10.1093/pcp/pcg072;
RA Hause B., Hause G., Kutter C., Miersch O., Wasternack C.;
RT "Enzymes of jasmonate biosynthesis occur in tomato sieve elements.";
RL Plant Cell Physiol. 44:643-648(2003).
CC -!- FUNCTION: Cytochrome P450 of the CYP74A subfamily involved in the
CC biosynthesis of jasmonic acid from lipoxygenase-derived hydroperoxides
CC of free fatty acids. Catalyzes the synthesis of unstable allene oxide,
CC which is further converted spontaneously by hydrolysis or cyclization.
CC Metabolizes 13- but not 9-hydroperoxides of linoleic and linolenic
CC acids. Can use 15S-hydroperoxy-11(Z),13(E),17(Z)-eicosatrienoic acid
CC (15-HPET) and 13S-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid
CC (13-HPOT) as substrates, but only 50% activity with 13S-hydroperoxy-
CC 9(Z),11(E)-octadecadienoic acid (13-HPOD).
CC {ECO:0000269|PubMed:10859201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate =
CC (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O;
CC Xref=Rhea:RHEA:25074, ChEBI:CHEBI:15377, ChEBI:CHEBI:36438,
CC ChEBI:CHEBI:58757; EC=4.2.1.92;
CC Evidence={ECO:0000269|PubMed:10859201};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:11154338}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11154338}; Stromal side
CC {ECO:0000269|PubMed:11154338}.
CC -!- TISSUE SPECIFICITY: Expressed in flower buds, leaves, roots, stems,
CC petioles and cotyledons (PubMed:10859201). Not detected in ripe fruits
CC (PubMed:10859201). Expressed in sieve elements (PubMed:12826630).
CC {ECO:0000269|PubMed:10859201, ECO:0000269|PubMed:12826630}.
CC -!- INDUCTION: Up-regulated by wounding in local and systemic leaves.
CC {ECO:0000269|PubMed:10859201}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 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; AF230371; AAF67141.1; -; mRNA.
DR RefSeq; NP_001274707.1; NM_001287778.2.
DR AlphaFoldDB; Q9LLB0; -.
DR SMR; Q9LLB0; -.
DR STRING; 4081.Solyc11g069800.1.1; -.
DR PaxDb; Q9LLB0; -.
DR PRIDE; Q9LLB0; -.
DR EnsemblPlants; Solyc11g069800.1.1; Solyc11g069800.1.1.1; Solyc11g069800.1.
DR GeneID; 101266902; -.
DR Gramene; Solyc11g069800.1.1; Solyc11g069800.1.1.1; Solyc11g069800.1.
DR KEGG; sly:101266902; -.
DR eggNOG; ENOG502QQNS; Eukaryota.
DR HOGENOM; CLU_045757_0_0_1; -.
DR InParanoid; Q9LLB0; -.
DR OMA; TEFFLRY; -.
DR OrthoDB; 485250at2759; -.
DR PhylomeDB; Q9LLB0; -.
DR Proteomes; UP000004994; Chromosome 11.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009978; F:allene oxide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Heme; Iron;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Membrane; Metal-binding;
KW Oxylipin biosynthesis; Plant defense; Plastid; Plastid inner membrane;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 32..510
FT /note="Allene oxide synthase 2, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436191"
FT BINDING 465
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q96242"
FT MUTAGEN 465
FT /note="C->A: Loss of heme binding and loss of activity, but
FT no effect on chloroplast import."
FT /evidence="ECO:0000269|PubMed:11154338"
SQ SEQUENCE 510 AA; 57203 MW; 3AF5A3DA9A9808AC CRC64;
MALTLSFSLP LPSLHQKIPS KYSTFRPIIV SLSDKSTIEI TQPIKLSTRT IPGDYGLPGI
GPWKDRLDYF YNQGKNDFFE SRIAKYKSTI FRTNMPPGPF ITSNPKVIVL LDGKSFPVLF
DASKVEKKDL FTGTFVPSTE LTGGYRILSY LDPSEPNHEK LKKLMFFLLS SRRDHVIPEF
HETYTELFET LDKEMEEKGT VGFNSGSDQA AFNFLARSLF GVNPVETKLG TDGPALIGKW
ILLQLHPVIT LGLPKFLDDV LLHTFRLPPI LVKKDYQRLY DFFYTNSANL FIEAEKLGIS
KDEACHNLLF ATCFNSFGGM KIFFPNMLKS IAKAGVEIHT RLANEIRSEV KSAGGKITMS
AMEKMPLMKS VVYEALRVDP PVASQYGRAK QDLKIESHDA VFEVKKGEIL FGYQPFATKD
PKIFDRPGEF VADRFVGEEG EKLLKHVLWS NGPETESPTV GNKQCAGKDF VVMVSRLFVT
EFFLRYGTLN VDVGTSALGS SITITSLKKA
