ID C74A2_PARAR Reviewed; 473 AA.
AC Q40778;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-MAY-2023, entry version 106.
DE RecName: Full=Allene oxide synthase;
DE EC=4.2.1.92;
DE AltName: Full=Cytochrome P450 74A2;
DE AltName: Full=Rubber particle protein;
DE Short=RPP;
GN Name=CYP74A2; Synonyms=RPP30;
OS Parthenium argentatum (Guayule rubber plant).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Parthenium.
OX NCBI_TaxID=35935;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 130-154; 253-282;
RP 328-344 AND 372-407.
RC STRAIN=cv. Line 11591; TISSUE=Stem bark;
RX PubMed=7721745; DOI=10.1074/jbc.270.15.8487;
RA Pan Z., Durst F., Werck-Reichhart D., Gardner H.W., Camara B., Cornish K.,
RA Backhaus R.A.;
RT "The major protein of guayule rubber particles is a cytochrome P450.
RT Characterization based on cDNA cloning and spectroscopic analysis of the
RT solubilized enzyme and its reaction products.";
RL J. Biol. Chem. 270:8487-8494(1995).
RN [2]
RP SEQUENCE REVISION.
RA Backhaus R.A.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 332-350; 353-368 AND 407-423.
RX PubMed=9660772; DOI=10.1074/jbc.273.29.18139;
RA Pan Z., Camara B., Gardner H.W., Backhaus R.A.;
RT "Aspirin inhibition and acetylation of the plant cytochrome P450, allene
RT oxide synthase, resembles that of animal prostaglandin endoperoxide H
RT synthase.";
RL J. Biol. Chem. 273:18139-18145(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE
RP ANALOG.
RX PubMed=18787124; DOI=10.1073/pnas.0804099105;
RA Li L., Chang Z., Pan Z., Fu Z.-Q., Wang X.;
RT "Modes of heme binding and substrate access for cytochrome P450 CYP74A
RT revealed by crystal structures of allene oxide synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13883-13888(2008).
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 (By similarity). {ECO:0000250}.
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: Note=Rubber particle.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; X78166; CAA55025.2; -; mRNA.
DR PIR; A56377; A56377.
DR PDB; 3DAM; X-ray; 2.40 A; A=1-473.
DR PDB; 3DAN; X-ray; 1.80 A; A=1-473.
DR PDB; 3DBM; X-ray; 2.60 A; A=1-473.
DR PDBsum; 3DAM; -.
DR PDBsum; 3DAN; -.
DR PDBsum; 3DBM; -.
DR AlphaFoldDB; Q40778; -.
DR SMR; Q40778; -.
DR UniPathway; UPA00382; -.
DR EvolutionaryTrace; Q40778; -.
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 CDD; cd11071; CYP74; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR PANTHER; PTHR24286:SF330; CYTOCHROME P450-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Metal-binding; Oxylipin biosynthesis.
FT CHAIN 1..473
FT /note="Allene oxide synthase"
FT /id="PRO_0000052128"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="substrate"
FT BINDING 275..276
FT /ligand="substrate"
FT BINDING 282
FT /ligand="substrate"
FT BINDING 343..346
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 426
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 CONFLICT 392
FT /note="Y -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="E -> EE (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:3DAN"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:3DAN"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:3DAN"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:3DAN"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 137..159
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:3DAN"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 276..295
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 297..314
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:3DBM"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 346..353
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:3DAN"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:3DAN"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:3DAN"
FT HELIX 399..407
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:3DAM"
FT HELIX 429..446
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 447..455
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:3DAN"
FT STRAND 462..471
FT /evidence="ECO:0007829|PDB:3DAN"
SQ SEQUENCE 473 AA; 53476 MW; 658D396763ECAA90 CRC64;
MDPSSKPLRE IPGSYGIPFF QPIKDRLEYF YGTGGRDEYF RSRMQKYQST VFRANMPPGP
FVSSNPKVIV LLDAKSFPIL FDVSKVEKKD LFTGTYMPST KLTGGYRVLS YLDPSEPRHA
QLKNLLFFML KNSSNRVIPQ FETTYTELFE GLEAELAKNG KAAFNDVGEQ AAFRFLGRAY
FNSNPEETKL GTSAPTLISS WVLFNLAPTL DLGLPWFLQE PLLHTFRLPA FLIKSTYNKL
YDYFQSVATP VMEQAEKLGV PKDEAVHNIL FAVCFNTFGG VKILFPNTLK WIGLAGENLH
TQLAEEIRGA IKSYGDGNVT LEAIEQMPLT KSVVYESLRI EPPVPPQYGK AKSNFTIESH
DATFEVKKGE MLFGYQPFAT KDPKVFDRPE EYVPDRFVGD GEALLKYVWW SNGPETESPT
VENKQCAGKD FVVLITRLFV IELFRRYDSF EIELGESPLG AAVTLTFLKR ASI
//
