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 27-MAR-2024, entry version 96. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 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 //