FMO1_PIG
ID FMO1_PIG Reviewed; 532 AA.
AC P16549;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 1;
DE EC=1.14.13.8;
DE AltName: Full=Dimethylaniline oxidase 1;
DE AltName: Full=Hepatic flavin-containing monooxygenase 1;
DE Short=FMO 1;
GN Name=FMO1; Synonyms=FMO-1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 137-151 AND 309-318.
RC TISSUE=Liver;
RX PubMed=2322534; DOI=10.1021/bi00453a014;
RA Gasser R., Tynes R.E., Lawton M.P., Korsmeyer K.K., Ziegler D.M.,
RA Philpot R.M.;
RT "The flavin-containing monooxygenase expressed in pig liver: primary
RT sequence, distribution, and evidence for a single gene.";
RL Biochemistry 29:119-124(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-14 AND 185-202, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=2383273; DOI=10.1016/0006-291x(90)92181-x;
RA Guan S.H., Falick A.M., Cashman J.R.;
RT "N-terminus determination: FAD and NADP binding domain mapping of hog liver
RT flavin-containing monooxygenase by tandem mass spectrometry.";
RL Biochem. Biophys. Res. Commun. 170:937-943(1990).
RN [3]
RP PROTEIN SEQUENCE OF 186-208.
RC TISSUE=Liver;
RX PubMed=7758472; DOI=10.1111/j.1432-1033.1995.tb20523.x;
RA Wu R.-F., Ichikawa Y.;
RT "An essential lysyl residue (Lys208) in the substrate-binding site of
RT porcine FAD-containing monooxygenase.";
RL Eur. J. Biochem. 229:749-753(1995).
RN [4]
RP GLYCOSYLATION AT ASN-120.
RX PubMed=9778310; DOI=10.1021/tx980117p;
RA Korsmeyer K.K., Guan S., Yang Z.C., Falick A.M., Ziegler D.M.,
RA Cashman J.R.;
RT "N-glycosylation of pig flavin-containing monooxygenase form 1:
RT determination of the site of protein modification by mass spectrometry.";
RL Chem. Res. Toxicol. 11:1145-1153(1998).
CC -!- FUNCTION: This protein is involved in the oxidative metabolism of a
CC variety of xenobiotics such as drugs and pesticides.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:Q95LA2}; Single-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q95LA2}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Liver.
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; M32031; AAA31033.1; -; mRNA.
DR PIR; A33768; A33768.
DR RefSeq; NP_999229.1; NM_214064.1.
DR RefSeq; XP_005656702.1; XM_005656645.2.
DR AlphaFoldDB; P16549; -.
DR SMR; P16549; -.
DR STRING; 9823.ENSSSCP00000016191; -.
DR iPTMnet; P16549; -.
DR PaxDb; P16549; -.
DR PeptideAtlas; P16549; -.
DR PRIDE; P16549; -.
DR Ensembl; ENSSSCT00000016637; ENSSSCP00000016191; ENSSSCG00000015268.
DR Ensembl; ENSSSCT00005029955; ENSSSCP00005018242; ENSSSCG00005018850.
DR Ensembl; ENSSSCT00005029982; ENSSSCP00005018261; ENSSSCG00005018850.
DR Ensembl; ENSSSCT00005030014; ENSSSCP00005018283; ENSSSCG00005018850.
DR Ensembl; ENSSSCT00005030021; ENSSSCP00005018288; ENSSSCG00005018850.
DR Ensembl; ENSSSCT00035075473; ENSSSCP00035030726; ENSSSCG00035056479.
DR Ensembl; ENSSSCT00045057157; ENSSSCP00045039947; ENSSSCG00045033391.
DR Ensembl; ENSSSCT00050083786; ENSSSCP00050035963; ENSSSCG00050061478.
DR Ensembl; ENSSSCT00055024748; ENSSSCP00055019643; ENSSSCG00055012560.
DR Ensembl; ENSSSCT00065045563; ENSSSCP00065019538; ENSSSCG00065033525.
DR Ensembl; ENSSSCT00065045579; ENSSSCP00065019546; ENSSSCG00065033525.
DR Ensembl; ENSSSCT00065045588; ENSSSCP00065019551; ENSSSCG00065033525.
DR Ensembl; ENSSSCT00070043455; ENSSSCP00070036573; ENSSSCG00070021841.
DR Ensembl; ENSSSCT00070043463; ENSSSCP00070036581; ENSSSCG00070021841.
DR Ensembl; ENSSSCT00070043480; ENSSSCP00070036597; ENSSSCG00070021841.
DR GeneID; 397132; -.
DR KEGG; ssc:397132; -.
DR CTD; 2326; -.
DR VGNC; VGNC:88170; FMO1.
DR eggNOG; KOG1399; Eukaryota.
DR GeneTree; ENSGT00940000160945; -.
DR HOGENOM; CLU_006909_8_2_1; -.
DR InParanoid; P16549; -.
DR OMA; VMIKEVN; -.
DR OrthoDB; 405736at2759; -.
DR TreeFam; TF105285; -.
DR Reactome; R-SSC-217271; FMO oxidises nucleophiles.
DR SABIO-RK; P16549; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Proteomes; UP000314985; Chromosome 9.
DR Bgee; ENSSSCG00000015268; Expressed in lung and 43 other tissues.
DR ExpressionAtlas; P16549; baseline and differential.
DR Genevisible; P16549; SS.
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: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; IDA:BHF-UCL.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0070995; P:NADPH oxidation; IDA:BHF-UCL.
DR GO; GO:0006082; P:organic acid metabolic process; IDA:BHF-UCL.
DR GO; GO:0009404; P:toxin metabolic process; IDA:BHF-UCL.
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; IPR002253; Flavin_mOase_1.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01121; FMOXYGENASE1.
DR SUPFAM; SSF51905; SSF51905; 3.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Endoplasmic reticulum; FAD;
KW Flavoprotein; Glycoprotein; Membrane; Microsome; Monooxygenase; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2383273"
FT CHAIN 2..532
FT /note="Dimethylaniline monooxygenase [N-oxide-forming] 1"
FT /id="PRO_0000147641"
FT TRANSMEM 511..531
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 SITE 208
FT /note="Important for substrate binding"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2383273"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:9778310"
SQ SEQUENCE 532 AA; 59952 MW; 5E475E7F2F3B8A67 CRC64;
MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYKSVVS
NSCKEMSCYP DFPFPEDYPN YVPNSHFLEY LRMYANQFNL LKCIQFKTKV CSVTKHEDFN
TTGQWDVVTL CEGKQESAVF DAVMVCTGFL TNPYLPLDSF PGINTFKGQY FHSRQYKHPD
IFKDKSVLVV GMGNSGTDIA VEASHLAKKV FLSTTGGAWV ISRVFDSGYP WDMVFMTRFQ
NMFRNSLPTP IVNWLIAKKM NSWFNHANYG LIPEDRIQLR EPVLNDELPG RIITGKVLIK
PSIKEVKENS VVFNSSPEEE PIDIIVFATG YTFAFPFLDE SVVKVEDGQA SLYKYIFPAH
LQKPTLAVIG LIKPLGSLLP TGDTQARWAV RVLKGVNKLP PSSVMIQEVN TRKENKPSGF
GLCYCKALQS DYIAYIDELL TYIDAKPNMF SLLLTDPHLA LTIFFGPCTP YQFRLTGPGK
WEGARNAIMT QWDRTFKVTK TRIVKESPSP FASLLKLFSF LALLVAIFQI FL
