FMO2_GORGO
ID FMO2_GORGO Reviewed; 535 AA.
AC Q8HZ69;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 109.
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 Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Furnes B., Sommer S., Feng J., Schlenk D.;
RT "Sequencing of pulmonary flavin-containing monooxygenase (FMO2) from
RT gorilla.";
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}.
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DR EMBL; AY132306; AAN06320.1; -; Genomic_DNA.
DR EMBL; AY132299; AAN06320.1; JOINED; Genomic_DNA.
DR EMBL; AY132300; AAN06320.1; JOINED; Genomic_DNA.
DR EMBL; AY132301; AAN06320.1; JOINED; Genomic_DNA.
DR EMBL; AY132302; AAN06320.1; JOINED; Genomic_DNA.
DR EMBL; AY132303; AAN06320.1; JOINED; Genomic_DNA.
DR EMBL; AY132304; AAN06320.1; JOINED; Genomic_DNA.
DR EMBL; AY132305; AAN06320.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q8HZ69; -.
DR SMR; Q8HZ69; -.
DR STRING; 9593.ENSGGOP00000008691; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_8_2_1; -.
DR InParanoid; Q8HZ69; -.
DR OMA; DCYERET; -.
DR Proteomes; UP000001519; 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: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:0070995; P:NADPH oxidation; ISS:UniProtKB.
DR Gene3D; 3.50.50.60; -; 4.
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_0000147645"
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; 60866 MW; B74F5608F5B51DD3 CRC64;
MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGV WRFKENVEDG RASIYQSVVT
NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV LSVRKCPDFS
SSGQWKVVTQ SNGKEQNAVF DAVMVCSGHH ILPHIPLKSF PGIERFKGQY FHSRQYKHPD
GFEGKRILVI GMGNSGSDIA VELSKNAAQV FISTRHGTWV MSRISEDGYP WDAVFHTRFR
SMLRNVLPRT AVKWMIEQQM NRWFNHENYG LEPQNKYIMK EPVLNDDVPS RLLCGAIKVK
STVKELTETS AIFEDGTVEE NIDVIIFATG YSFSFPFLED SLVKVENNMV SLYKYIFPAH
LDKSTLACIG LIQPLGSIFP TAELQARWVT RVFKGLCSLP SERTMMMDII KRNEKRIDLF
GESQSQTLQT NYVDYLDELA LEIGAKPDFC SLLFKDPKLA VRLYFGPCNS YQYRLVGPGQ
WEGARNAILT QKQRILKPLK TRALKDSSNF SVSFLLKILG LLAVVVAFFC QLQWS
