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C74A2_PARAR
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-AUG-2022, entry version 102.
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   PRIDE; 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   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   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
 
 
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