ID   CP6B3_PAPPO             Reviewed;         498 AA.
AC   Q27756; Q95038;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Cytochrome P450 6B3;
DE            EC=1.14.14.1;
DE   AltName: Full=CYP6B3v1/CYP6B3v2;
DE   AltName: Full=CYPVIB3;
GN   Name=CYP6B3;
OS   Papilio polyxenes (Black swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=7146;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (CYP6B3V1).
RX   PubMed=8589841; DOI=10.1111/j.1365-2583.1995.tb00020.x;
RA   Hung C.F., Harrison T.L., Berenbaum M.R., Schuler M.A.;
RT   "CYP6B3: a second furanocoumarin-inducible cytochrome P450 expressed in
RT   Papilio polyxenes.";
RL   Insect Mol. Biol. 4:149-160(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CYP6B3V2).
RX   PubMed=8901557; DOI=10.1073/pnas.93.22.12200;
RA   Hung C.F., Holzmacher R., Connolly E., Berenbaum M.R., Schuler M.A.;
RT   "Conserved promoter elements in the CYP6B gene family suggest common
RT   ancestry for cytochrome P450 monooxygenases mediating furanocoumarin
RT   detoxification.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12200-12205(1996).
CC   -!- FUNCTION: Enables the insect to feed on furanocoumarin-producing plants
CC       and evolved as an adaptation for detoxification of xanthotoxin and
CC       other furanocoumarins.
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; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- INDUCTION: By xanthotoxin and bergapten (linear furanocoumarins) as
CC       well as by angelicin and sphondin (angular furanocoumarins).
CC   -!- POLYMORPHISM: The sequence shown is that of 6B3-1, 6B3-2 seems to
CC       differ in 17 positions and is probably an allele.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U25819; AAA96255.1; -; mRNA.
DR   EMBL; U65488; AAB06741.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q27756; -.
DR   SMR; Q27756; -.
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:SF103; CYTOCHROME P450 6A14-LIKE PROTEIN-RELATED; 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..498
FT                   /note="Cytochrome P450 6B3"
FT                   /id="PRO_0000051895"
FT   BINDING         443
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         47
FT                   /note="A -> V (in 6B3-2)"
FT   VARIANT         52
FT                   /note="P -> H (in 6B3-2)"
FT   VARIANT         82
FT                   /note="L -> I (in 6B3-2)"
FT   VARIANT         92..93
FT                   /note="PT -> LI (in 6B3-2)"
FT   VARIANT         98
FT                   /note="P -> S (in 6B3-2)"
FT   VARIANT         108
FT                   /note="L -> I (in 6B3-2)"
FT   VARIANT         289
FT                   /note="T -> I (in 6B3-2)"
FT   VARIANT         350
FT                   /note="G -> S (in 6B3-2)"
FT   VARIANT         354..357
FT                   /note="FLGR -> YLSK (in 6B3-2)"
FT   VARIANT         395..397
FT                   /note="IIV -> VII (in 6B3-2)"
FT   VARIANT         401
FT                   /note="G -> S (in 6B3-2)"
SQ   SEQUENCE   498 AA;  57473 MW;  9BC760ACBEB657BC CRC64;
     MLYVITLVTV LAGLLHYYFT RNFDYWKKRN VAGPKPIPFF GNLKDSALRR KPQVMVYKSI
     YDEFPNEKVV GIYRMTTPSV LLRDLDIIKH VPTKDFEPFA DRGVEFSLDG LGANIFHADG
     DRWRSLRNRF TPLFTSGKLK TMLPLMSQVG DKFINTSDEV SQTKSEQSIH DLVQIFTITN
     IAACAFGLNL DENMLKTLQD LDKYIFTVNY SGEFDMLYPG ILKKFNGSIF PKVVKQFFDK
     LTKDIFEMRK GTSSCQKDMI DSIQELRQQK TVDLWRKHDN EDVKPLELTD GVISAQMFIF
     YAAGYETSAT TMTYLFYELA KNPDIQDKLI AEIDEVLSRH DGNITYECLG EMTFLGRVFD
     ETLRKYPVGD FTQRNAKTDY VFPGTDITIK KGQTIIVSTW GIQNDPKYYP NPEKFDPERF
     NPENIKNRHP CAYLPFSAGP RNCLGLRFAK WQIEVCVVKV LSKYRVEPSN KSSGEFKFDP
     MRLFVLPKGG IFVNIVRR
//