ID A5HG32_BOMMO Unreviewed; 503 AA.
AC A5HG32;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Cytochrome P450 monooxygenase CYP4M5 {ECO:0000313|EMBL:ABP99018.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000313|EMBL:ABP99018.1};
RN [1] {ECO:0000313|EMBL:ABP99018.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Laos {ECO:0000313|EMBL:ABP99018.1};
RA Wang D., Li B., Chen Y.H., Wei Z.G., Zhao H.Q., Xu Y.X., Wang W.B.,
RA Gong C.L., Shen W.D.;
RT "Molecular cloning and analysis of two closely linked P450 genes from
RT Bombyx mori and their expression patterns.";
RL Submitted (MAR-2007) 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 -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; EF528484; ABP99018.1; -; mRNA.
DR AlphaFoldDB; A5HG32; -.
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; cd20628; CYP4; 1.
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 PANTHER; PTHR24291:SF105; CYTOCHROME P450 4P1-RELATED; 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 Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
SQ SEQUENCE 503 AA; 58310 MW; 358E7078CE470475 CRC64;
MFVYLIFIAS FFLLIHLAFN YNSKAVMMNK VPGPKLSFIL GNAPEIMMLS SVELMKLARK
FASRWDGIYR IWAFPLSIIN IYNPDDVEVI VSTTKHNEKS SVYKFLKPWL GDGLLISKGE
KWQQRRKILT PAFHFNILRQ FSVIIEENSQ RLVESLEKCV GKPTDIVPVV SEYTLNSICE
TSMGTQLSDK TEDAWKAYKD AIYELGPYFF QRFTRVYLYF DIIFYLTSLW RKMKKPLKSL
HGFTSTVIKE RKIYVEQNGV KFGEDVNDDD LYIYKKRRKT AMLDLLIAAQ KDGEIDDHGI
QEEVDTFMFE GHDTTASGLT FCFMLLANHR AVQDKIVEEI NDTMGDSTRR ANLEDLSKMK
YLECCIKESL RLYPPVHFIS RNLNESVVLS NYEIPAGSFC HIHIFDLHRR ADIYEDPLVY
DPDRFSQENS KGRHPYAYIP FSAGPRNCIG QKFAMIEMKS AVAEVLRKYE LVPVTRPSEI
ELIADIILRH SGPVEITFNK RTK
//
