ID   CP6B7_HELAM             Reviewed;         504 AA.
AC   O61387;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Cytochrome P450 6B7;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPVIB7;
GN   Name=CYP6B7;
OS   Helicoverpa armigera (Cotton bollworm) (Heliothis armigera).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Helicoverpa.
OX   NCBI_TaxID=29058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9753767; DOI=10.1016/s0965-1748(98)00045-9;
RA   Ranasinghe C., Hobbs A.A.;
RT   "Isolation and characterization of two cytochrome P450 cDNA clones for
RT   CYP6B6 and CYP6B7 from Helicoverpa armigera (Hubner): possible involvement
RT   of CYP6B7 in pyrethroid resistance.";
RL   Insect Biochem. Mol. Biol. 28:571-580(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Peripheral membrane protein {ECO:0000305}. Microsome membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC   -!- INDUCTION: By treatment with the monoterpene, alpha-pinene.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF031468; AAC09227.1; -; mRNA.
DR   AlphaFoldDB; O61387; -.
DR   SMR; O61387; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase 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:0050896; P:response to stimulus; IEA:UniProt.
DR   CDD; cd11056; CYP6-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; PTHR24292; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24292:SF105; CYTOCHROME P450 9AC1; 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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN           1..504
FT                   /note="Cytochrome P450 6B7"
FT                   /id="PRO_0000051899"
FT   BINDING         445
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"
SQ   SEQUENCE   504 AA;  58218 MW;  9EC92687CF4A0A4A CRC64;
     MWVLYLPAVL SVLIVTLYLY FTRTFNYWKK RNVRGPEPTV FFGNLKDSTL RKKNIGIVME
     EIYNQFPYEK VVGMYRMTTP CLLVRDFHVI KHIMIKDFEA FRDRGVEFSK EGLGQNLFHA
     DGETWRALRN RFTPIFTSGK LKNMFYLMHE GADNFIDHVS KECEKKQEFE VHSLLQTYTM
     STISSCAFGV SYNSISDKVQ TLEIVDKIIS EPSYAIELDY MYPKLLAKLN LSIIPTPVQH
     FFKSLVDNII SQRNGKPAGR NDFMDLILEL RQMGEVTSNK YLDGVTSLEI TDEVICAQAF
     VFYVAGYETS ATTMSYLIYQ LSLNQDVQNK LIAEVDEAIK ASDGKVTYDT VKEMKYLNKV
     FDETLRMYSI VEPLQRKATR DYQIPGTDVV IEKDTMVLIS PRGIHYDPKY YDNPKQFNPD
     RFDAEEVGKR HPCAYLPFGL GQRNCIGMRF GRLQSLLCIT KILSKFRIEP SKNTDRNLQV
     EPRRVTIGPK GGIRVNIVPR KIVS
//