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Methyl farnesoate epoxidase (EC 1.14.13.202) (Cytochrome P450 CYP15A1)

 C15A1_DIPPU             Reviewed;         493 AA.
Q6R7M4;
22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 59.
RecName: Full=Methyl farnesoate epoxidase {ECO:0000305};
EC=1.14.13.202 {ECO:0000269|PubMed:15024118};
AltName: Full=Cytochrome P450 CYP15A1 {ECO:0000303|PubMed:15024118};
Flags: Precursor;
Name=CYP15A1 {ECO:0000303|PubMed:15024118};
Diploptera punctata (Pacific beetle cockroach).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Polyneoptera; Dictyoptera; Blattodea;
Blaberoidea; Blaberidae; Diplopterinae; Diploptera.
NCBI_TaxID=6984;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND TISSUE
SPECIFICITY.
TISSUE=Corpora allata;
PubMed=15024118; DOI=10.1073/pnas.0306980101;
Helvig C., Koener J.F., Unnithan G.C., Feyereisen R.;
"CYP15A1, the cytochrome P450 that catalyzes epoxidation of methyl
farnesoate to juvenile hormone III in cockroach corpora allata.";
Proc. Natl. Acad. Sci. U.S.A. 101:4024-4029(2004).
-!- FUNCTION: Catalyzes the conversion of methyl farnesoate to
juvenile hormone III acid (methyl (2E,6E)-(10R)-10,11-epoxy-
3,7,11-trimethyl-2,6-dodecadienoate) in juvenile hormone
biosynthesis. {ECO:0000269|PubMed:15024118}.
-!- CATALYTIC ACTIVITY: Methyl (2E,6E)-farnesoate + NADPH + O(2) =
juvenile hormone III + NADP(+) + H(2)O.
{ECO:0000269|PubMed:15024118}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:P04798};
-!- ENZYME REGULATION: Inhibited by substituted imidazole inhibitors
TH27, KK96 and KK71. {ECO:0000269|PubMed:15024118}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=380 uM for methyl (2E,6E)-farnesoate (with purified enzyme)
{ECO:0000269|PubMed:15024118};
KM=26 uM for methyl (2E,6E)-farnesoate (with recombinant enzyme
expressed in E.coli) {ECO:0000269|PubMed:15024118};
-!- TISSUE SPECIFICITY: Specifically expressed in the corpora allata
of at the time of maximal juvenile hormone production by the
glands. {ECO:0000269|PubMed:15024118}.
-!- MISCELLANEOUS: The enzyme is present in all insects, except in
lepidoptera (moths and butterflies), and is specific for methyl
farnesoate. Lepidoptera contain the farnesoate epoxidase, which is
specific for farnesoate. {ECO:0000305}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; AY509244; AAS13464.1; -; mRNA.
ProteinModelPortal; Q6R7M4; -.
SMR; Q6R7M4; -.
KEGG; ag:AAS13464; -.
KO; K14937; -.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
GO; GO:0006718; P:juvenile hormone biosynthetic process; IDA:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Glycoprotein; Heme; Iron; Metal-binding; Monooxygenase; NADP;
Oxidoreductase; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 493 Methyl farnesoate epoxidase.
{ECO:0000255}.
/FTId=PRO_0000433620.
METAL 438 438 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P04798}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 458 458 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
SEQUENCE 493 AA; 56523 MW; 7D6F3D8DD4D171A0 CRC64;
MVIALIVIII FLVCLDVIKP RGYPPGPVWL PVVGSYLWFR REKSRVGYYH LVWSSLSSRY
GPVTGMRLGT DYIVVACGYD AIRDILLRDE FDGRPDGYFF RLRTFGKRMG VVFTDGPVWQ
EQRRFCMQHL RKLGLGSRSM EAHIEEEARD LVASLHRRSN GGLTAIPMHD VFDICVLNSL
WAMLAGHRFD LDDQRLVDLL DIVHKCFRMI DPSGGLLNQM PPLRFIAPRH SGYTNLMTHL
NRIWNFLRET IDDHRKSFNA DNMRDLIDLF LREMETSKCQ NNSSFEDLQL VSLCLDLFMA
GSETTSNTLG FAVLYMLLYP QVQRRVQDEL DRCVGTDRQP TLQDRRSLRY LEAVLMEIQR
HATIAPSGIP HKALKNTVLM GHTIPKGTTV LVSMWSLHRD VQHWGDPEVF RPERFISGNG
NIKQDDWFMP FGIGKRRCIG ETLAKASLFL FFSTLLHNFS ILPSSESPLP SLEGYDGVTL
SPKPFSAKLI PRK


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