CP6B3_PAPPO
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 03-AUG-2022, entry version 96.
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 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..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