CP6B5_PAPGL
ID CP6B5_PAPGL Reviewed; 476 AA.
AC Q95036;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cytochrome P450 6B5;
DE EC=1.14.14.1;
DE AltName: Full=CYP6B5v1;
DE AltName: Full=CYPVIB5;
DE Flags: Fragment;
GN Name=CYP6B5;
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].
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 furnocoumarin.
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; U65490; AAB06743.1; -; Genomic_DNA.
DR AlphaFoldDB; Q95036; -.
DR SMR; Q95036; -.
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..>476
FT /note="Cytochrome P450 6B5"
FT /id="PRO_0000051897"
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 NON_TER 476
SQ SEQUENCE 476 AA; 55102 MW; 7E6F7E733645229D CRC64;
MLTIFIVTAT LFAILYLYFT RNFNYWKDRN VVGPEPTVFF GNIMESVIRR KHLIMIYKDI
YEAFPKEKVV GIYRMTTPCL LLRDLDVIKH VMIKDFDLFN DRGVEFSEEG LGLNIFHADG
DRWRVLRQCF TPLFTSGKLK NMLNLMSDRG DKFIKMVEKI CDKEPEQQII PLVRKFTMAS
ITTCAFGMEL DEEMIETLDK LDSLIFTTSY GNEIDMMYPG ILKKLNSSLF SKMIAPFFDN
LTKTIIEQRG GKPTNRKDLM DLILELRQKK AIEPMKKTHD EQVTTLELTD SVIAAQTFIF
YAAGYETSAS TMSFLLFELA ENPDIQEKVI AEVDETLKRH NGEITYDTLS EMTYLTQVFH
ETLRKYPVAD ILLRNAKADY AVPGTNVTLK KGQTVVVSGF GIHYDPKYYP DPEKFDPERF
SPENVRNRHP CAYIPFGAGQ RKCLGMRFGQ WQVQVCIIKL LSKFRFEPST KTMSEF
