C15A1_DIPPU
ID C15A1_DIPPU Reviewed; 493 AA.
AC Q6R7M4;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Methyl farnesoate epoxidase {ECO:0000305};
DE EC=1.14.14.127 {ECO:0000269|PubMed:15024118};
DE AltName: Full=Cytochrome P450 CYP15A1 {ECO:0000303|PubMed:15024118};
DE Flags: Precursor;
GN Name=CYP15A1 {ECO:0000303|PubMed:15024118};
OS Diploptera punctata (Pacific beetle cockroach).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Blaberidae;
OC Diplopterinae; Diploptera.
OX NCBI_TaxID=6984;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC TISSUE=Corpora allata;
RX PubMed=15024118; DOI=10.1073/pnas.0306980101;
RA Helvig C., Koener J.F., Unnithan G.C., Feyereisen R.;
RT "CYP15A1, the cytochrome P450 that catalyzes epoxidation of methyl
RT farnesoate to juvenile hormone III in cockroach corpora allata.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4024-4029(2004).
CC -!- FUNCTION: Catalyzes the conversion of methyl farnesoate to juvenile
CC hormone III acid (methyl (2E,6E)-(10R)-10,11-epoxy-3,7,11-trimethyl-
CC 2,6-dodecadienoate) in juvenile hormone biosynthesis.
CC {ECO:0000269|PubMed:15024118}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=methyl (2E,6E)-farnesoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = H(+) + H2O + juvenile hormone III + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:43728, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27493, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:80535; EC=1.14.14.127;
CC Evidence={ECO:0000269|PubMed:15024118};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- ACTIVITY REGULATION: Inhibited by substituted imidazole inhibitors
CC TH27, KK96 and KK71. {ECO:0000269|PubMed:15024118}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=380 uM for methyl (2E,6E)-farnesoate (with purified enzyme)
CC {ECO:0000269|PubMed:15024118};
CC KM=26 uM for methyl (2E,6E)-farnesoate (with recombinant enzyme
CC expressed in E.coli) {ECO:0000269|PubMed:15024118};
CC -!- TISSUE SPECIFICITY: Specifically expressed in the corpora allata of at
CC the time of maximal juvenile hormone production by the glands.
CC {ECO:0000269|PubMed:15024118}.
CC -!- MISCELLANEOUS: The enzyme is present in all insects, except in
CC lepidoptera (moths and butterflies), and is specific for methyl
CC farnesoate. Lepidoptera contain the farnesoate epoxidase, which is
CC specific for farnesoate. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AY509244; AAS13464.1; -; mRNA.
DR AlphaFoldDB; Q6R7M4; -.
DR SMR; Q6R7M4; -.
DR KEGG; ag:AAS13464; -.
DR BRENDA; 1.14.14.127; 1963.
DR SABIO-RK; Q6R7M4; -.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR 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.
DR GO; GO:0006718; P:juvenile hormone biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..493
FT /note="Methyl farnesoate epoxidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433620"
FT BINDING 438
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:P04798"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ 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
