FMO2_MACMU
ID FMO2_MACMU Reviewed; 535 AA.
AC Q28505;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
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:0000269|PubMed:11302936};
DE EC=1.14.13.8 {ECO:0000269|PubMed:11302936};
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9061021; DOI=10.1016/s0167-4781(97)00004-3;
RA Yueh M.-F., Krueger S.K., Williams D.E.;
RT "Pulmonary flavin-containing monooxygenase (FMO) in rhesus macaque:
RT expression of FMO2 protein, mRNA and analysis of the cDNA.";
RL Biochim. Biophys. Acta 1350:267-271(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11302936;
RA Krueger S.K., Yueh M.F., Martin S.R., Pereira C.B., Williams D.E.;
RT "Characterization of expressed full-length and truncated FMO2 from rhesus
RT monkey.";
RL Drug Metab. Dispos. 29:693-700(2001).
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:0000269|PubMed:11302936}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-
CC dimethylaniline N-oxide + NADP(+); Xref=Rhea:RHEA:24468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16269, ChEBI:CHEBI:17735, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.13.8;
CC Evidence={ECO:0000269|PubMed:11302936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24469;
CC Evidence={ECO:0000305|PubMed:11302936};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=670 uM for N,N-dimethylaniline {ECO:0000269|PubMed:11302936};
CC KM=1700 uM for (S)-nicotine {ECO:0000269|PubMed:11302936};
CC KM=760 uM for nitro- 5-thiobenzoate (TNB) (with methimazole-dependent
CC oxidation and western blotting estimation)
CC {ECO:0000269|PubMed:11302936};
CC KM=744 uM for nitro- 5-thiobenzoate (TNB) (with methimazole-dependent
CC oxidation and flavin estimation) {ECO:0000269|PubMed:11302936};
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; U59453; AAB02939.1; -; mRNA.
DR RefSeq; NP_001036242.1; NM_001042777.1.
DR AlphaFoldDB; Q28505; -.
DR SMR; Q28505; -.
DR STRING; 9544.ENSMMUP00000025933; -.
DR GeneID; 703639; -.
DR KEGG; mcc:703639; -.
DR CTD; 2327; -.
DR eggNOG; KOG1399; Eukaryota.
DR InParanoid; Q28505; -.
DR Proteomes; UP000006718; 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; -; 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 1: Evidence at protein 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_0000147647"
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; 60961 MW; 85621203B07CCFAE CRC64;
MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGV WRFKEKVEDG RASIYQSVVT
NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV LSVRKCPDFS
SSGQWKVVTQ SNGKEQSAVF DAVMVCTGHH FLPHIPLKSF PGIERFKGQY FHSRQYKHPD
GFEGKRILVI GMGNSGSDIA VELSKSAAQV FISTRHGTWV MSRVSEDGYP WDSVFHTRFR
SMLRNVLPRT VVKWMIEQQM NQWFNHENYG LEPQNKYIMK EPVLNDDVPS RLLCGAIKVK
STVKELTETS AIFEDGTVEE NIDVIIFATG YSFSFPFLED SLVKVENNMV SLYKYIFPAH
LEKSTFACIG LIQPLGSIFP TAELQARWVT RVFKGLCHLP SERTMMMDII KRNEKRIDLF
GESQSQTLQT NYVDYLDELA LEIGAKPDFC SLLFKDPKLA VRLFFGPCNS YQYRLAGPGQ
WEGARSAIFT QKQRILKPLK TRVLKDSSNF PVSFLLKILG LVAVVVAFFC QLQWS
