ID   A0A9E8BWL7_9NEOP        Unreviewed;       470 AA.
AC   A0A9E8BWL7;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   27-NOV-2024, entry version 8.
DE   SubName: Full=Cytochrome P450 CYP4XF3 {ECO:0000313|EMBL:UZE89878.1};
OS   Chrysoperla zastrowi sillemi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Neuroptera; Hemerobiiformia; Chrysopidae;
OC   Chrysopinae; Chrysoperla.
OX   NCBI_TaxID=482137 {ECO:0000313|EMBL:UZE89878.1};
RN   [1] {ECO:0000313|EMBL:UZE89878.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Pathak J., Ramasamy G.G., Agrawal A., Srivastava S., Basavaarya B.R.,
RA   Muthugounder M., Muniyappa V.K., Maria P., Rai A., Venkatesan T.;
RT   "Comparative Transcriptome Analysis to Reveal Differentially Expressed
RT   cytochrome P450 in Response to Imidacloprid in the Aphid Lion, Chrysoperla
RT   zastrowi sillemi (Esben-Petersen).";
RL   Insects 13:0-0(2022).
RN   [2] {ECO:0000313|EMBL:UZE89878.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Pathak J., Thiruvengadam V., Gracy G.R.;
RL   Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the metabolism of insect hormones and in
CC       the breakdown of synthetic insecticides.
CC       {ECO:0000256|ARBA:ARBA00003690}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602401-1};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004406}. Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004174}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; ON646362; UZE89878.1; -; mRNA.
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   Gene3D; 1.10.630.10; Cytochrome P450; 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   InterPro; IPR050196; Cytochrome_P450_Monoox.
DR   PANTHER; PTHR24291:SF189; CYTOCHROME P450 4V2; 1.
DR   PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022848};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602401-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602401-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602401-1,
KW   ECO:0000256|RuleBase:RU000461}; Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          39..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          174..201
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         412
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:0000256|PIRSR:PIRSR602401-1"
SQ   SEQUENCE   470 AA;  53638 MW;  2F8F2AA339DBC6C0 CRC64;
     MDDDAMNIKQ QEQQNDKQTT TTILINNNHE EEEVYTTINN NNNNTTTTIS DNEQQQQPQQ
     SINRNTWSRT SLRRSPIHNN NGGGTGSGSI KRWGSFRTTN KRQLGSNALA SELYRSSSFN
     CTSGSGGNVT TRTTNCNLDD RMSTTSKDDL YGCSSMTTTY SSMSDHDQDI IDHGSLLEDD
     VLDLNHKVEQ LQQQVNILTS TTIEQQQHLN NNNINNNINN NNNNIIDDNS NVCLGSKKRI
     IFLDLLLQST HLSGEPLTDK EIIDEVTNFM FAGHDTTSVQ LSLLMYLLCE HPEIQNELYK
     EQCAILTDIN GDPSFKQIQE MNYLERTIKE SQRILPCVIS FSRKMTADIQ LKTNNLLLPK
     GCTASIFVYD VHHNPKIYEN PEKFDPDRFL PENIRGRHPY AYIPFSAGPR NCLGQKFALL
     EMKTVMSNII RNFKILPAYE DNGDKFKPIF RRYMLLTSLN GIQIRLESRR
//