AOS3_SOLLC
ID AOS3_SOLLC Reviewed; 491 AA.
AC Q8GZP5;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Allene oxide synthase 3 {ECO:0000303|PubMed:12351632};
DE Short=LeAOS3 {ECO:0000303|PubMed:12351632};
DE EC=4.2.1.92 {ECO:0000269|PubMed:12351632};
DE AltName: Full=Allene oxide cyclase {ECO:0000303|PubMed:12351632};
DE EC=5.3.99.6 {ECO:0000269|PubMed:12351632};
DE AltName: Full=Cytochrome P450 CYP74C3 {ECO:0000303|PubMed:12351632};
DE AltName: Full=Cytochrome P450 CYP74D1 {ECO:0000303|PubMed:17073790};
GN Name=AOS3 {ECO:0000303|PubMed:12351632};
GN Synonyms=CYP74C3 {ECO:0000303|PubMed:12351632},
GN CYP74D1 {ECO:0000303|PubMed:17073790}; OrderedLocusNames=Solyc10g007960;
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,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Castlemart;
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 [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 NOMENCLATURE.
RX PubMed=17073790; DOI=10.1042/bst0341223;
RA Hughes R.K., Belfield E.J., Casey R.;
RT "CYP74C3 and CYP74A1, plant cytochrome P450 enzymes whose activity is
RT regulated by detergent micelle association, and proposed new rules for the
RT classification of CYP74 enzymes.";
RL Biochem. Soc. Trans. 34:1223-1227(2006).
RN [4]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=18780387; DOI=10.1002/cbic.200800331;
RA Grechkin A.N., Mukhtarova L.S., Latypova L.R., Gogolev Y., Toporkova Y.Y.,
RA Hamberg M.;
RT "Tomato CYP74C3 is a multifunctional enzyme not only synthesizing allene
RT oxide but also catalyzing its hydrolysis and cyclization.";
RL ChemBioChem 9:2498-2505(2008).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF PHE-295 AND SER-297.
RX PubMed=18789329; DOI=10.1016/j.febslet.2008.09.005;
RA Toporkova Y.Y., Gogolev Y.V., Mukhtarova L.S., Grechkin A.N.;
RT "Determinants governing the CYP74 catalysis: conversion of allene oxide
RT synthase into hydroperoxide lyase by site-directed mutagenesis.";
RL FEBS Lett. 582:3423-3428(2008).
CC -!- FUNCTION: Cytochrome P450 metabolizing both 13- and 9-hydroperoxides of
CC linoleic and linolenic acids, but with a marked preference for 9-
CC hydroperoxy fatty acids (PubMed:12351632, PubMed:18780387). Has no
CC activity toward 13S-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid
CC (13-HPOT) (PubMed:18780387). Catalyzes not only the synthesis of allene
CC oxide, but also its hydrolysis and cyclization (PubMed:18780387). The
CC first step is the synthesis of (12Z)-9,10-epoxyoctadeca-10,12-dienoic
CC acid (9,10-EOD) and the final products are (9R)-alpha-ketol and the
CC racemic cis-10-oxo-11-phytoenoic acid (PubMed:18780387). The cyclase
CC activity possesses regiospecificity and (9Z)-12,13-epoxyoctadeca-9,11-
CC dienoic acid (12,13-EOD) is significantly less efficient as a substrate
CC for cyclopentenone production than 9,10-EOD (PubMed:18780387). Has no
CC hydroperoxide lyase activity (PubMed:12351632). May play a defensive
CC role against soil-borne pests that affect roots or juvenile tissues as
CC they emerge from the germinating seed (PubMed:12351632).
CC {ECO:0000269|PubMed:12351632, ECO:0000269|PubMed:18780387}.
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:12351632};
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 Evidence={ECO:0000269|PubMed:12351632};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for (10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate (9-HPOD)
CC {ECO:0000269|PubMed:12351632};
CC KM=16 uM for (10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate
CC (9-HPOT) {ECO:0000269|PubMed:12351632};
CC KM=11 uM for (9Z,11E)-(13S)-hydroperoxyoctadeca-9,11-dienoate (13-
CC HPOD) {ECO:0000269|PubMed:12351632};
CC KM=4 uM for (9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate
CC (13-HPOT) {ECO:0000269|PubMed:12351632};
CC Note=kcat is 820 sec(-1) with 9-HPOD as substrate. kcat is 236 sec(-
CC 1) with 9-HPOT as substrate. kcat is 99 sec(-1) with 13-HPOD as
CC substrate. kcat is 21 sec(-1) with 13-HPOT as substrate.
CC {ECO:0000269|PubMed:12351632};
CC -!- TISSUE SPECIFICITY: Expressed in roots. Not detected in aerial tissues,
CC including cotyledons, leaves, stems and flower buds.
CC {ECO:0000269|PubMed:12351632}.
CC -!- DEVELOPMENTAL STAGE: Expressed early after seed germination, when the
CC radical has just emerged from the seed coat.
CC {ECO:0000269|PubMed:12351632}.
CC -!- INDUCTION: Not induced in wounded or jasmonate-treated leaves.
CC {ECO:0000269|PubMed:12351632}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF454634; AAN76867.1; -; mRNA.
DR RefSeq; NP_001265949.1; NM_001279020.2.
DR AlphaFoldDB; Q8GZP5; -.
DR SMR; Q8GZP5; -.
DR STRING; 4081.Solyc10g007960.1.1; -.
DR PaxDb; Q8GZP5; -.
DR PRIDE; Q8GZP5; -.
DR EnsemblPlants; Solyc10g007960.1.1; Solyc10g007960.1.1.1; Solyc10g007960.1.
DR GeneID; 101247264; -.
DR Gramene; Solyc10g007960.1.1; Solyc10g007960.1.1.1; Solyc10g007960.1.
DR KEGG; sly:101247264; -.
DR eggNOG; ENOG502QV50; Eukaryota.
DR HOGENOM; CLU_045757_0_0_1; -.
DR InParanoid; Q8GZP5; -.
DR OMA; FCEGKNP; -.
DR OrthoDB; 759497at2759; -.
DR PhylomeDB; Q8GZP5; -.
DR Proteomes; UP000004994; Chromosome 10.
DR GO; GO:0009978; F:allene oxide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046423; F:allene-oxide cyclase 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; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Heme; Iron; Isomerase;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Metal-binding;
KW Oxylipin biosynthesis; Plant defense; Reference proteome.
FT CHAIN 1..491
FT /note="Allene oxide synthase 3"
FT /id="PRO_0000436192"
FT BINDING 444
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 295
FT /note="F->I: Loss of AOS activity, but gain of a
FT hydroperoxide lyase activity."
FT /evidence="ECO:0000269|PubMed:18789329"
FT MUTAGEN 297
FT /note="S->A: Strongly decreased AOS activity, but gain of a
FT hydroperoxide lyase activity."
FT /evidence="ECO:0000269|PubMed:18789329"
SQ SEQUENCE 491 AA; 55514 MW; 0B3C778CC6C7683C CRC64;
MANTKDSYHI ITMDTKESSI PSLPMKEIPG DYGVPFFGAI KDRYDFHYNQ GADEFFRSRM
KKYDSTVFRT NVPPGPFNAR NSKVVVLVDA VSYPILFDNS QVDKENYFEG TFMSSPSFNG
GYKVCGFLGT SDPKHTTLKG LFLSTLTRLH DKFIPIFTTS ITSMFTSLEK ELSEKGTSYF
NPIGDNLSFE FLFRLFCEGK NPIDTSVGPN GPKIVDKWVF LQLAPLISLG LKFVPNFLED
LVLHTFPLPY ILVKRDHQKL YNAFYNSMKD ILDEAEKLGV KRDEACHNFV FLAGFNSYGG
LKVFFPSLIK WIGTSGPSLH ARLVKEIRTA VKEAGGVTLS AIDKMPLVKS VVYETLRMDP
PVPFQTVKAR KNIIITNHES SFLIKKDELI FGYQPLATKD SKVFKNAEEF NPDRFVGGGE
KLLKYVYWSN GKEIDNPSVN DKQCPGKDLI VLMGRLLVVE FFMRYDTFEV EFGKLLLGSK
VTFKSLTKAT S
