CP6A1_MUSDO
ID CP6A1_MUSDO Reviewed; 509 AA.
AC P13527;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cytochrome P450 6A1;
DE EC=1.14.14.1;
DE AltName: Full=CYPVIA1;
GN Name=CYP6A1;
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2922393; DOI=10.1073/pnas.86.5.1465;
RA Feyereisen R., Koener J.F., Farnsworth D.E., Nebert D.W.;
RT "Isolation and sequence of cDNA encoding a cytochrome P-450 from an
RT insecticide-resistant strain of the house fly, Musca domestica.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1465-1469(1989).
CC -!- FUNCTION: Involved in the metabolism of insect hormones and in the
CC breakdown of synthetic insecticides.
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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; L27242; AAA72423.1; -; Genomic_DNA.
DR EMBL; M25367; AAA29293.1; -; mRNA.
DR PIR; A32157; A32157.
DR RefSeq; NP_001274159.1; NM_001287230.1.
DR AlphaFoldDB; P13527; -.
DR SMR; P13527; -.
DR PRIDE; P13527; -.
DR GeneID; 101889365; -.
DR KEGG; mde:101889365; -.
DR VEuPathDB; VectorBase:MDOA014776; -.
DR eggNOG; KOG0158; Eukaryota.
DR Proteomes; UP000095301; Whole Genome Shotgun Assembly.
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..509
FT /note="Cytochrome P450 6A1"
FT /id="PRO_0000051865"
FT BINDING 449
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 CONFLICT 70..73
FT /note="DPLP -> GPFA (in Ref. 1; AAA29293)"
FT /evidence="ECO:0000305"
FT CONFLICT 372..373
FT /note="Missing (in Ref. 1; AAA29293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 58731 MW; 229EF807F1DFF8F5 CRC64;
MDFGSFLLYA LGVLASLALY FVRWNFGYWK RRGIPHEEPH LVMGNVKGLR SKYHIGEIIA
DYYRKFKGSD PLPGIFLGHK PAAVVLDKEL RKRVLIKDFS NFANRGLYYN EKDDPLTGHL
VMVEGEKWRS LRTKLSPTFT AGKMKYMYNT VLEVGQRLLE VMYEKLEVSS ELDMRDILAR
FNTDVIGSVA FGIECNSLRN PHDRFLAMGR KSIEVPRHNA LIMAFIDSFP ELSRKLGMRV
LPEDVHQFFM SSIKETVDYR EKNNIRRNDF LDLVLDLKNN PESISKLGGL TFNELAAQVF
VFFLGGFETS SSTMGFALYE LAQNQQLQDR LREEVNEVFD QFKEDNISYD ALMNIPYLDQ
VLNETLRKYP VGVGSALTRQ TLNDYVVPHN PKYVLPKGTL VFIPVLGIHY DPELYPNPEE
FDPERFSPEM VKQRDSVDWL GFGDGPRNCI GMRFGKMQSR LGLALVIRHF RFTVCSRTDI
PMQINPESLA WTPKNNLYLN VQAIRKKIK