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Database: UniProt
Entry: A0A2A3EBU3_APICC
LinkDB: A0A2A3EBU3_APICC
Original site: A0A2A3EBU3_APICC 
ID   A0A2A3EBU3_APICC        Unreviewed;       419 AA.
AC   A0A2A3EBU3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN   ORFNames=APICC_09888 {ECO:0000313|EMBL:PBC29207.1};
OS   Apis cerana cerana (Oriental honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Apis.
OX   NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC29207.1, ECO:0000313|Proteomes:UP000242457};
RN   [1] {ECO:0000313|EMBL:PBC29207.1, ECO:0000313|Proteomes:UP000242457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC29207.1};
RA   Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA   Wu J.;
RT   "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT   insights into honey bee biology.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU361177};
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC       ECO:0000256|RuleBase:RU361177}.
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DR   EMBL; KZ288291; PBC29207.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3EBU3; -.
DR   STRING; 94128.A0A2A3EBU3; -.
DR   Proteomes; UP000242457; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 2.
DR   PIRSF; PIRSF000332; FMO; 2.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU361177};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361177};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU361177}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361177};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242457}.
SQ   SEQUENCE   419 AA;  48298 MW;  5F25674BAD1F1635 CRC64;
     MKIAVIGAGS AGLAALRHCT SDIYDTQVIC YEKTDQVGGT WVYREETGLD RYGLPIHTSM
     YKNLRTNLPK EVMGYPDYSV PDNPDSYLTR TQILEFLNSY CDHFNLRQYI QFLHNVELVE
     PSVGDRKWMI KVKDLKRNII LEESFDAVMV CNGHYFEPSI PNLKGQKIFQ GEQLHSHDYR
     VPDIFTDKTV VVLGAGPSGM DLALEISKKA KRIILSHHLK DPIGTVFPDN VVQKPDVKEL
     TKHGVLFKDD TNESVDAIFY CTGYKYSFPF LSEKCGVRVD SNMVTPLWKH LISIENPTLA
     LIGLPFYVCA FSMFDLQVRF VLRYWSGKKN FPPKADMLKE ETQELESRKK EGLQKKHFHM
     MGFKQDHYYD DLANTAGITP LPPVLTKLHN ESSLLFLDDL VHYREKRYKI IDDYNFIQL
//
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