C15C1_BOMMO
ID C15C1_BOMMO Reviewed; 493 AA.
AC C0SPF7; H9JQA2; L0N4L5; L0N734; L0N7A3;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 2.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Farnesoate epoxidase {ECO:0000305};
DE EC=1.14.14.128 {ECO:0000269|PubMed:22412378};
DE AltName: Full=Cytochrome P450 15C1 {ECO:0000303|PubMed:22412378};
DE AltName: Full=Protein dimolting {ECO:0000303|PubMed:22412378};
DE Short=mod {ECO:0000303|PubMed:22412378};
DE Flags: Precursor;
GN Name=CYP15C1 {ECO:0000303|PubMed:22412378}; ORFNames=BGIBMGA011708;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Kinshu X Showa; TISSUE=Corpora allata;
RX PubMed=22412378; DOI=10.1371/journal.pgen.1002486;
RA Daimon T., Kozaki T., Niwa R., Kobayashi I., Furuta K., Namiki T.,
RA Uchino K., Banno Y., Katsuma S., Tamura T., Mita K., Sezutsu H.,
RA Nakayama M., Itoyama K., Shimada T., Shinoda T.;
RT "Precocious metamorphosis in the juvenile hormone-deficient mutant of the
RT silkworm, Bombyx mori.";
RL PLoS Genet. 8:E1002486-E1002486(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T;
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
CC -!- FUNCTION: Catalyzes the conversion of farnesoate to juvenile hormone
CC III acid in juvenile hormone biosynthesis.
CC {ECO:0000269|PubMed:22412378}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = H(+) + H2O + juvenile hormone III carboxylate + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:43724, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:83274, ChEBI:CHEBI:83276;
CC EC=1.14.14.128; Evidence={ECO:0000269|PubMed:22412378};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- TISSUE SPECIFICITY: constitutively expressed in corpora allata from the
CC first instar larval to adult stages. {ECO:0000269|PubMed:22412378}.
CC -!- DISRUPTION PHENOTYPE: Larvae undergo precocious metamorphosis in the
CC third (dimolter) or fourth instar (trimolter).
CC {ECO:0000269|PubMed:22412378}.
CC -!- MISCELLANEOUS: The enzyme is specifically found in lepidoptera (moths
CC and butterflies) and is specific for farnesoate. Other insects contain
CC the methyl farnesoate epoxidase, which is specific for methyl
CC farnesoate. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB124839; BAH47266.1; -; mRNA.
DR EMBL; AK289312; BAM73839.1; -; mRNA.
DR EMBL; AK289313; BAM73840.1; -; mRNA.
DR EMBL; AK289314; BAM73841.1; -; mRNA.
DR RefSeq; NP_001140197.1; NM_001146725.1.
DR AlphaFoldDB; C0SPF7; -.
DR SMR; C0SPF7; -.
DR STRING; 7091.BGIBMGA011708-TA; -.
DR GeneID; 100286798; -.
DR KEGG; bmor:100286798; -.
DR CTD; 100286798; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_22_3_1; -.
DR OrthoDB; 702827at2759; -.
DR BRENDA; 1.14.14.128; 890.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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 GO; GO:0007552; P:metamorphosis; IMP: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 Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..493
FT /note="Farnesoate epoxidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433621"
FT BINDING 433
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 CONFLICT 6
FT /note="V -> A (in Ref. 1; BAM73840)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="D -> E (in Ref. 1; BAH47266/BAM73839/BAM73840/
FT BAM73841)"
FT CONFLICT 197
FT /note="E -> K (in Ref. 1; BAH47266/BAM73839/BAM73840/
FT BAM73841)"
FT CONFLICT 215
FT /note="F -> I (in Ref. 1; BAH47266/BAM73839/BAM73840/
FT BAM73841)"
FT CONFLICT 281
FT /note="P -> L (in Ref. 1; BAH47266/BAM73839/BAM73840/
FT BAM73841)"
FT CONFLICT 336
FT /note="P -> H (in Ref. 1; BAH47266/BAM73839/BAM73840/
FT BAM73841)"
SQ SEQUENCE 493 AA; 57206 MW; 2D3ACA494889B87E CRC64;
MLALIVLCFI LFFYIISRRH RGLCYPPGPT PLPIVGNLLS VLWESRKFKC HHLIWQSWSQ
KYGNLLGLRL GSINVVVVTG IELIREVSNR EVFEGRPDGF FYTMRSFGKK LGLVFSDGPT
WHRTRRFVLK YLKNFGYNSR FMNVYIGDEC EALVQLRLAD AGEPILVNQM FHITIVNILW
RLVAGKRYDL EDQRLKELCS LVMRLFKLVD MSGGFLNFLP FLRHFVPRLI GFTELQEIHN
ALHQYLREII KEHQENLQLG APKDVIDAFL IDMLESQDDK PTLDDLQVVC LDLLEAGMET
VTNTAVFMLL HVVRNEDVQR KLHQEIDDII GRDRNPLLDD RIRMVYTEAV ILETLRISTV
ASMGIPHMAL NDAKLGNYII PKGTFILLSL YELHHGPHWK DPETFRPERF LTKEGNILQD
EWLIPFGIGK RRCIGEGLAR SELFMFLTHI LQKFHLRIPK NEPLPSTEPI DGLSLSAKQF
RIIFEPRKTF KSI
