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Database: UniProt
Entry: Q6R7M4
LinkDB: Q6R7M4
Original site: Q6R7M4 
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   27-MAR-2024, entry version 74.
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   GlyCosmos; Q6R7M4; 2 sites, No reported glycans.
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   CDD; cd20651; CYP15A1-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24300:SF380; CYTOCHROME P450 15A1; 1.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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
//
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