ID   CP74_LINUS              Reviewed;         536 AA.
AC   P48417;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Allene oxide synthase, chloroplastic;
DE            EC=4.2.1.92;
DE   AltName: Full=Cytochrome P450 74A;
DE   AltName: Full=Hydroperoxide dehydrase;
DE   Flags: Precursor;
GN   Name=CYP74A; Synonyms=CYP74;
OS   Linum usitatissimum (Flax) (Linum humile).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Linaceae; Linum.
OX   NCBI_TaxID=4006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Embryo;
RX   PubMed=8378325; DOI=10.1073/pnas.90.18.8519;
RA   Song W.-C., Funk C.D., Brash A.R.;
RT   "Molecular cloning of an allene oxide synthase: a cytochrome P450
RT   specialized for the metabolism of fatty acid hydroperoxides.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:8519-8523(1993).
CC   -!- FUNCTION: Involved in the biosynthesis of jasmonic acid, a growth
CC       regulator that is implicated also as a signaling molecule in plant
CC       defense. Acts on a number of unsaturated fatty-acid hydroperoxides,
CC       forming the corresponding allene oxides.
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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U00428; AAA03353.1; -; mRNA.
DR   AlphaFoldDB; P48417; -.
DR   SMR; P48417; -.
DR   UniPathway; UPA00382; -.
DR   GO; GO:0009507; C:chloroplast; 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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
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; Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW   Lyase; Metal-binding; Oxylipin biosynthesis; Plastid; Transit peptide.
FT   TRANSIT         1..58
FT                   /note="Chloroplast"
FT   CHAIN           59..536
FT                   /note="Allene oxide synthase, chloroplastic"
FT                   /id="PRO_0000003626"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         338..339
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         406..409
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         489
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"
FT   VARIANT         525
FT                   /note="S -> T"
SQ   SEQUENCE   536 AA;  59670 MW;  6B44ED84552986D5 CRC64;
     MASSALNNLV AVNPNTLSPS PKSTPLPNTF SNLRRVSAFR PIKASLFGDS PIKIPGITSQ
     PPPSSDETTL PIRQIPGDYG LPGIGPIQDR LDYFYNQGRE EFFKSRLQKY KSTVYRANMP
     PGPFIASNPR VIVLLDAKSF PVLFDMSKVE KKDLFTGTYM PSTELTGGYR ILSYLDPSEP
     NHTKLKQLLF NLIKNRRDYV IPEFSSSFTD LCEVVEYDLA TKGKAAFNDP AEQAAFNFLS
     RAFFGVKPID TPLGKDAPSL ISKWVLFNLA PILSVGLPKE VEEATLHSVR LPPLLVQNDY
     HRLYEFFTSA AGSVLDEAEQ SGISRDEACH NILFAVCFNS WGGFKILFPS LMKWIGRAGL
     ELHTKLAQEI RSAIQSTGGG KVTMAAMEQM PLMKSVVYET LRIEPPVALQ YGKAKKDFIL
     ESHEAAYQVK EGEMLFGYQP FATKDPKIFD RPEEFVADRF VGEGVKLMEY VMWSNGPETE
     TPSVANKQCA GKDFVVMAAR LFVVELFKRY DSFDIEVGTS SLGASITLTS LKRSTF