CP6B4_PAPGL
ID CP6B4_PAPGL Reviewed; 500 AA.
AC Q27902; Q95035;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cytochrome P450 6B4;
DE EC=1.14.14.1;
DE AltName: Full=CYP6B4v1/CYP6B4v2;
DE AltName: Full=CYPVIB4;
GN Name=CYP6B4;
OS Papilio glaucus (Eastern tiger swallowtail butterfly) (Pterourus glaucus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio; Pterourus.
OX NCBI_TaxID=45779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9219364; DOI=10.1016/s0965-1748(97)00009-x;
RA Hung C.F., Berenbaum M.R., Schuler M.A.;
RT "Isolation and characterization of CYP6B4, a furanocoumarin-inducible
RT cytochrome P450 from a polyphagous caterpillar (Lepidoptera:
RT Papilionidae).";
RL Insect Biochem. Mol. Biol. 27:377-385(1997).
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. This isozyme metabolizes isopimpinellin,
CC imperatorin, and bergapten at high rates, xanthotoxin and psoralen at
CC intermediate rates and angelicin, sphondin, and trioxsalen only at very
CC low rates.
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 furnocoumarin.
CC -!- POLYMORPHISM: The sequence shown is that of 6B4-1, 6B4-2 seems to
CC differ in 7 positions and is probably an allele.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; U47059; AAB05892.1; -; mRNA.
DR EMBL; U65489; AAB06742.1; -; Genomic_DNA.
DR AlphaFoldDB; Q27902; -.
DR SMR; Q27902; -.
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..500
FT /note="Cytochrome P450 6B4"
FT /id="PRO_0000051896"
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 17
FT /note="F -> L (in 6B4-2)"
FT VARIANT 160
FT /note="F -> I (in 6B4-2)"
FT VARIANT 229
FT /note="I -> L (in 6B4-2)"
FT VARIANT 286
FT /note="L -> F (in 6B4-2)"
FT VARIANT 477
FT /note="N -> S (in 6B4-2)"
FT VARIANT 481
FT /note="K -> T (in 6B4-2)"
FT VARIANT 496
FT /note="I -> L (in 6B4-2)"
SQ SEQUENCE 500 AA; 58046 MW; F6042D7E196029E2 CRC64;
MLTIFIVTAT LFAILYFYFT RNFNYWKDRN VVGPEPTVFF GNIMESVIRR KHLIMIYKDI
YEAFPKEKVV GIYRMTTPCL LLRDLDVIKH VMIKDFDLFN DRGVEFSEEG LGLNIFHADG
DRWRVLRQCF TPLFTSGKLK NMLNLMSDRG DKFIKMVEKF CDKEPEQQII PLVRKFTMAS
ITTCAFGMEL DEEMIETLDK LDSLIFTTSY GNEIDMMYPG ILKKLNSSIF SKMIAPFFDN
LTKTIIEQRG GKPTNRKDLM DLILELRQKK AIEPMKKTHD EQVTTLELTD SVIAAQTFIF
YAAGYETSAS TMSFLLFELA ENPDIQEKVI AEVDETLKRH NGEITYDTLS EMTYLTQVFH
ETLRKYPVAD ILLRNAKADY AVPGTNVTLK KGQTVVVSGF GIHYDPKYYP DPEKFDPERF
SPENVRNRHP CAYIPFGAGQ RKCLGMRFGQ WQVQVCIIKL LSKFRFEPST KTMSEFNYDP
KRLLVYPKSG IFLNIIPRNY