ID   CP6J1_BLAGE             Reviewed;         501 AA.
AC   Q964R1;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Cytochrome P450 6j1;
DE            EC=1.14.-.-;
DE   AltName: Full=CYPVIJ1;
GN   Name=CYP6J1;
OS   Blattella germanica (German cockroach) (Blatta germanica).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Blattellidae;
OC   Blattella.
OX   NCBI_TaxID=6973;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11422508; DOI=10.1046/j.1365-2583.2001.00247.x;
RA   Wen Z., Scott J.G.;
RT   "Cloning of two novel P450 cDNAs from German cockroaches, Blattella
RT   germanica (L.): CYP6K1 and CYP6J1.";
RL   Insect Mol. Biol. 10:131-137(2001).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Peripheral membrane protein {ECO:0000305}. Microsome membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF281325; AAK57913.1; -; mRNA.
DR   AlphaFoldDB; Q964R1; -.
DR   SMR; Q964R1; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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; IPR002402; Cyt_P450_E_grp-II.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24292; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24292:SF105; CYTOCHROME P450 9AC1; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00464; EP450II.
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..501
FT                   /note="Cytochrome P450 6j1"
FT                   /id="PRO_0000051885"
FT   BINDING         444
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"
SQ   SEQUENCE   501 AA;  57918 MW;  265E97926D9CFE0E CRC64;
     MFEFGSIIVT VIAVFITIPI CLYLFLTRHF NFWKKRGVIY VRPLPFFGNL KDVLLQKKYI
     GYYLKDIYEE NINKPYVGIF AFDQPALLVN DLEIVKNILV KDSRNFIDRM VKVDESLSPL
     NANAIFALRG QKWKHVRTSL TPTFTTGKMK NMFYLVDKCG QQLVLFIEKF AKAENPVAVK
     DAVERFTMDV TAMCAFGIEC NSLQDPKAEF SNLLHRIFQL SFTSAVANLA TFFAPWVQNF
     FRLKLMDSEI EDRIRDIVWR AVHLREKTGE KRNDLLDYLM ELRTSETSKL DGDDFVAQAF
     GFLVAGFHTS SMTLTFALYE LSVHQDIQTT ARTEIKDVLE HHKKKVTYYS IKDMKYLDMV
     VNETLRKYPA IPFLDRRCQE DYPLTQDLML PAGTGVYIPV YALHHDSKYF PSPAKFDPER
     FSEKNKQNIP HFAYMPFGEG PRNCIGMRFG SMQVKAALIH ILSNFEVSPC KETRIPLIID
     PKPFNLMALG GVYLNITKFN N
//