FMO2_PANTR
ID FMO2_PANTR Reviewed; 535 AA.
AC Q8HZ70;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Furnes B., Sommer S., Feng J., Schlenk D.;
RT "Sequencing of exon 1-8 of pulmonary flavin-containing monooxygenase (FMO2)
RT from chimpanzee.";
RL Submitted (JUL-2002) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY132298; AAN06319.1; -; Genomic_DNA.
DR EMBL; AY132291; AAN06319.1; JOINED; Genomic_DNA.
DR EMBL; AY132292; AAN06319.1; JOINED; Genomic_DNA.
DR EMBL; AY132293; AAN06319.1; JOINED; Genomic_DNA.
DR EMBL; AY132294; AAN06319.1; JOINED; Genomic_DNA.
DR EMBL; AY132295; AAN06319.1; JOINED; Genomic_DNA.
DR EMBL; AY132296; AAN06319.1; JOINED; Genomic_DNA.
DR EMBL; AY132297; AAN06319.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001009008.1; NM_001009008.2.
DR AlphaFoldDB; Q8HZ70; -.
DR SMR; Q8HZ70; -.
DR STRING; 9598.ENSPTRP00000002780; -.
DR PaxDb; Q8HZ70; -.
DR Ensembl; ENSPTRT00000003028; ENSPTRP00000002780; ENSPTRG00000001672.
DR GeneID; 449587; -.
DR KEGG; ptr:449587; -.
DR CTD; 2327; -.
DR VGNC; VGNC:543; FMO2.
DR eggNOG; KOG1399; Eukaryota.
DR GeneTree; ENSGT00940000161099; -.
DR HOGENOM; CLU_006909_8_2_1; -.
DR InParanoid; Q8HZ70; -.
DR OMA; DCYERET; -.
DR OrthoDB; 405736at2759; -.
DR TreeFam; TF105285; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000001672; Expressed in lung and 13 other tissues.
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:0004497; F:monooxygenase activity; IBA:GO_Central.
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:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0070995; P:NADPH oxidation; ISS:UniProtKB.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; IEA:Ensembl.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:Ensembl.
DR GO; GO:0072592; P:oxygen metabolic process; IEA:Ensembl.
DR GO; GO:0009404; P:toxin metabolic process; IEA:Ensembl.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
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 3: Inferred from homology;
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_0000147649"
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; 60903 MW; 8D58AF9B2BDBF640 CRC64;
MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGV WRFKENVEDG RASIYQSVIT
NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV LSVRKCPDFS
SSGQWKVVTQ SNGKEQSAVF DAVMVCSGHH ILPHIPLKSF PGIERFKGQY FHSRQYKHPD
GFEGKRILVI GMGNSGSDIA VELSKNAAQV FISTRHGTWV MSRISEDGYP WDSVFHTRFR
SMLRNVLPRT AVKWMIEQQM NRWFNHENYG LEPQNKYIMK EPVLNDDVPS RLLCGAIKVK
STVKELTETS AIFEDGTVEE NIDVIIFATG YSFSFPFLED SLVKVENNMV SLYKYIFPAH
LDKSTLACIG LIQPLGSIFP TAELQARWVT RVFKGLCSLP SERTMMMDII KRNEKRIDLF
GESQSQTLQT NYVDYLDELA LEIGAKPDFC SLLFKDPKLA VRLYFGPCNS YQYRLVGPGQ
WEGARNAIFT QKQRILKPLK TRALKDSSNF SVSFLLKILG LLAVVVAFFC QLQWS
