ID   CP6B6_HELAM             Reviewed;         504 AA.
AC   Q95031;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Cytochrome P450 6B6;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPVIB6;
GN   Name=CYP6B6;
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U64800; AAB06441.1; -; mRNA.
DR   AlphaFoldDB; Q95031; -.
DR   SMR; Q95031; -.
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   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   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 6B6"
FT                   /id="PRO_0000051898"
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;  57602 MW;  28C7B95798518DB0 CRC64;
     MWIFYFPAVI SVLIVSLYFY FTRTFNYWKK RNVRGPEPTV FFGNLKDSAL PRKNMGVVME
     ELYNMFPEEK VIGIYRMTSP CLLVRDLEVI KHIMIKDFEV FSDRGVEFSK EGLGSNLFHA
     DGETWRALRN RFTPIFTSGK PKNMFYLMHE GADNFIDHVS AECEKNQEFE VHSLLQTYTM
     STIAACAFGI SYDSIGDKVK ALDIVDKIIS EPSYAIELDM MYPGLLSKLN LSIFPTAVKN
     FFKSLVDNIV AQRNGKPSGR NDFMDLILEL RQLGEVTSNK YGSSASSLEI TDEVICAQAF
     VFYIAGYETS ATTMAYMIYQ LALSPDIQNK LIAEVDEVLK ANDGKVTYDT VKEMKYMNKA
     FDETLRMYSI VEPLQRKATR DYKIPGTDVV IEKDTIVLIS PRGIHYDPKY YDNPKQFNPD
     RFDAEEVGKR HPCAYLPFGL GQRNCIGMRF GRLQSLLCIT KILSKFRIEP SKNTDRNLQV
     EPHRGLIGPK GGIRVNVVPR KLVS