ID   CP6B2_HELAM             Reviewed;         504 AA.
AC   Q27664;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Cytochrome P450 6B2;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPVIB2;
GN   Name=CYP6B2;
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].
RC   TISSUE=Midgut;
RX   PubMed=8541882; DOI=10.1016/0965-1748(95)00033-r;
RA   Wang X.P., Hobbs A.A.;
RT   "Isolation and sequence analysis of a cDNA clone for a pyrethroid inducible
RT   cytochrome P450 from Helicoverpa armigera.";
RL   Insect Biochem. Mol. Biol. 25:1001-1009(1995).
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 phenobarbital and the insecticide permethrin.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U18085; AAB60252.1; -; mRNA.
DR   AlphaFoldDB; Q27664; -.
DR   SMR; Q27664; -.
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 6B2"
FT                   /id="PRO_0000051894"
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"
FT   VARIANT         106
FT                   /note="L -> V"
FT   VARIANT         115
FT                   /note="Q -> S"
SQ   SEQUENCE   504 AA;  58218 MW;  C0BDF218509A8849 CRC64;
     MWIFYFPAVI SVLIVTLYFY FTRTFNYWKK RNVRGPEPVV FFGNLKDSAL RKKNMGVVME
     ELYNMFPEEK VIGIYRMTSP CLLVRDLEVI KHIMIKDFEV FSDRGLEFSK EGLGQNLFHA
     DGDTWRTLRN RFTPIFTSGK LKNMFYLMNE GADNFIDHVS KECEKHQEFE IHTLLQTYTM
     STISSCAFGV SYDTISDKLD TLAIVDKIIS EPSYAIELDM MYPGLLPKLN LSIFPSVVHK
     FFKNLVNTIV TQRNGKPSGR NDFMDLILEL RQMGEITSNK YGNNMSTLEI TESVMCAQAF
     VFYIAGYETS ATTMAYLTYQ LALNPDIQNK LIAEIDEAIK ANGGKVTYDT VKDMKYLNKV
     FDETLRMYSI VEPLQRKAIR DYKLPGTDVV IEKDTVVLIS PRGIHYDPKY YDNPKQFNPE
     RFFAEEVGKR HPCAYLPFGL GQRNCIGMRF GRLQSLLCIT KLLSKFRLEP SKNTDRNLQV
     EPYRFIIGPK GGIRLNIVPR KDVS
//