FMO1_RABIT
ID FMO1_RABIT Reviewed; 535 AA.
AC P17636;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 1;
DE EC=1.14.13.8;
DE AltName: Full=Dimethylaniline oxidase 1;
DE AltName: Full=FMO 1A1;
DE AltName: Full=FMO form 1;
DE Short=FMO 1;
DE AltName: Full=Hepatic flavin-containing monooxygenase 1;
GN Name=FMO1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white;
RX PubMed=2318837; DOI=10.1016/s0021-9258(19)39441-4;
RA Lawton M.P., Gasser R., Tynes R.E., Hodgson E., Philpot R.M.;
RT "The flavin-containing monooxygenase enzymes expressed in rabbit liver and
RT lung are products of related but distinctly different genes.";
RL J. Biol. Chem. 265:5855-5861(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-535, AND ACETYLATION AT ALA-2.
RC TISSUE=Liver;
RX PubMed=2355001; DOI=10.1016/s0021-9258(18)86945-9;
RA Ozols J.;
RT "Covalent structure of liver microsomal flavin-containing monooxygenase
RT form 1.";
RL J. Biol. Chem. 265:10289-10299(1990).
RN [3]
RP PROTEIN SEQUENCE OF 4-33 AND 224-247, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=2505769; DOI=10.1016/0006-291x(89)92097-4;
RA Ozols J.;
RT "Liver microsomes contain two distinct NADPH-Monooxygenases with NH2-
RT terminal segments homologous to the flavin containing NADPH-monooxygenase
RT of Pseudomonas fluorescens.";
RL Biochem. Biophys. Res. Commun. 163:49-55(1989).
CC -!- FUNCTION: This protein is involved in the oxidative metabolism of a
CC variety of xenobiotics such as drugs and pesticides. Form I catalyzes
CC the N-oxygenation of secondary and tertiary amines.
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 {ECO:0000269|PubMed:2505769};
CC Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000305|PubMed:2505769}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:2505769}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; M32030; AAA31278.1; -; mRNA.
DR PIR; A35182; A35182.
DR PIR; A35427; A35427.
DR RefSeq; NP_001075754.1; NM_001082285.2.
DR AlphaFoldDB; P17636; -.
DR SMR; P17636; -.
DR iPTMnet; P17636; -.
DR PRIDE; P17636; -.
DR GeneID; 100009120; -.
DR KEGG; ocu:100009120; -.
DR CTD; 2326; -.
DR eggNOG; KOG1399; Eukaryota.
DR InParanoid; P17636; -.
DR OrthoDB; 405736at2759; -.
DR Proteomes; UP000001811; 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: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 Gene3D; 3.50.50.60; -; 1.
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; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2355001"
FT CHAIN 2..535
FT /note="Dimethylaniline monooxygenase [N-oxide-forming] 1"
FT /id="PRO_0000147642"
FT TRANSMEM 514..534
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 /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2355001"
FT CONFLICT 20
FT /note="C -> S (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="E -> K (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="S -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="S -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="C -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="E -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="L -> M (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="F -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="S -> C (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="L -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="L -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="L -> LES (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 60183 MW; 8EE95683FC3E43D5 CRC64;
MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYKSVVS
NSCKEMSCYS DFPFPEDYPN YVPNSQFLDY LKMYADRFSL LKSIQFKTTV FSITKCQDFN
VSGQWEVVTL HEGKQESAIF DAVMVCTGFL TNPHLPLGCF PGIKTFKGQY FHSRQYKHPD
IFKDKRVLVV GMGNSGTDIA VEASHVAKKV FLSTTGGAWV ISRVFDSGYP WDMVFTTRFQ
NFIRNSLPTP IVTWLVAKKM NSWFNHANYG LVPKDRIQLK EPVLNDELPG RIITGKVFIR
PSIKEVKENS VVFGNAHNTP SEEPIDVIVF ATGYTFAFPF LDESVVKVED GQASLYKYIF
PAHLQKPTLA VIGLIKPLGS MLPTGETQAR YTVQVFKGVI KLPPTSVMIK EVNERKENKH
NGFGLCYCKA LQADYITYID DLLTSINAKP NLFSLLLTDP LLALTMFFGP YSPYQFRLTG
PGKWKGARNA IMTQWDRTFK VTKTRIVQES SSPFESLLKL FAVLALLVSV FLIFL
