ID   FMO2_PONAB              Reviewed;         535 AA.
AC   Q5REK0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 2 {ECO:0000250|UniProtKB:Q99518};
DE            EC=1.14.13.- {ECO:0000250|UniProtKB:Q99518};
DE   AltName: Full=Dimethylaniline oxidase 2;
DE   AltName: Full=FMO 1B1;
DE   AltName: Full=Pulmonary flavin-containing monooxygenase 2;
DE            Short=FMO 2;
GN   Name=FMO2 {ECO:0000250|UniProtKB:Q99518};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidative metabolism of numerous xenobiotics,
CC       including mainly therapeutic drugs and insecticides that contain a soft
CC       nucleophile, most commonly nitrogen and sulfur and participates to
CC       their bioactivation. {ECO:0000250|UniProtKB:Q99518}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane
CC       {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17635}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P17635}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR   EMBL; CR857525; CAH89807.1; -; mRNA.
DR   RefSeq; NP_001124835.1; NM_001131363.1.
DR   AlphaFoldDB; Q5REK0; -.
DR   SMR; Q5REK0; -.
DR   STRING; 9601.ENSPPYP00000000598; -.
DR   GeneID; 100171693; -.
DR   KEGG; pon:100171693; -.
DR   CTD; 2327; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   InParanoid; Q5REK0; -.
DR   OrthoDB; 405736at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0070995; P:NADPH oxidation; ISS:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   InterPro; IPR002254; Flavin_mOase_2.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01122; FMOXYGENASE2.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Isopeptide bond;
KW   Magnesium; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P17635"
FT   CHAIN           2..535
FT                   /note="Dimethylaniline monooxygenase [N-oxide-forming] 2"
FT                   /id="PRO_0000229039"
FT   TRANSMEM        510..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         9..13
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         32
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         40..41
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         60..61
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         61..62
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   BINDING         195..198
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P17635"
FT   CROSSLNK        492
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250|UniProtKB:Q99518"
SQ   SEQUENCE   535 AA;  60978 MW;  16FCCC733693E13D CRC64;
     MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGV WRFKENVEDG RASIYQSVVT
     NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV LSVRKCPDFS
     SSGQWKVVTQ SNSKEQSAVF DAVMVCSGHH ILPHIPLKSF PGIERFKGQY FHSRQYKHPD
     GFEGKRILVI GMGNSGSDIA VELSKNAAQV FISTRHGTWV LSRISEDGYP WDSVFHTRFR
     SMLRRVLPRT AVKWMIEQQM NRWFNHENYG LEPQNKYFMK EPVLNDDVPS RLLCGAIKVK
     STVKELTETS AIFEDGTVEE NIDVIIFATG YSFSFPFLED SLVKVENNMV SLYKYIFPAH
     LEKSTLACIG LIQPLGSIFP TAELQARWVT RVFKGLCSLP SERTMMMDII KRNEKRIELF
     GESQSQTLQT NYVDYLDELA LEIGAKPDFC SLLFKDPKLA VRLYFGPCNS YQYRLVGPGQ
     WEGARSAIFT QKQRILKPLK TRALKDSSNF SVSFLLKILG LLAVVVAFFC QLQWS