FMO2_CAVPO
ID FMO2_CAVPO Reviewed; 535 AA.
AC P36366; Q05194;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
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}; Synonyms=FMO-2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS 522-LEU AND 530-PHE, AND
RP POLYMORPHISM.
RC STRAIN=Hartley; TISSUE=Lung;
RX PubMed=1306120; DOI=10.1097/00008571-199210000-00003;
RA Nikbakht K.N., Lawton M.P., Philpot R.M.;
RT "Guinea pig or rabbit lung flavin-containing monooxygenases with distinct
RT mobilities in SDS-PAGE are allelic variants that differ at only two
RT positions.";
RL Pharmacogenetics 2:207-216(1992).
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 -!- TISSUE SPECIFICITY: Lung.
CC -!- POLYMORPHISM: There are two allelic forms (A and B) (PubMed:1306120).
CC {ECO:0000269|PubMed:1306120}.
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; L10037; AAB59631.1; -; Genomic_DNA.
DR AlphaFoldDB; P36366; -.
DR SMR; P36366; -.
DR STRING; 10141.ENSCPOP00000012602; -.
DR eggNOG; KOG1399; Eukaryota.
DR InParanoid; P36366; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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: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 2: Evidence at transcript 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_0000147644"
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"
FT VARIANT 522
FT /note="V -> L (in B form)"
FT /evidence="ECO:0000269|PubMed:1306120"
FT VARIANT 530
FT /note="S -> F (in B form)"
FT /evidence="ECO:0000269|PubMed:1306120"
SQ SEQUENCE 535 AA; 60942 MW; 10D9DDA06EB58DA2 CRC64;
MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGL WRFKENVEDG RASIYKSVIT
NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRLFAKKFDL LKYIQFQTTV LTVKKHPDFS
SSGQWEVVTQ SDGKEQSAVF DAVMVCSGHH ILPHIPLKSF PGIERFKGQY FHSRQYKHPA
GFEGKRILVI GIGNSASDIA SELSKNAAQV FISTRNGSWV MSRISEDGYP WDMVFHTRFK
SMLRNILPRT VSKWMMEQQL NRWFNHANYS LEPKNKYLMK EPILNDDLPS RILYGAVKVK
SRVTQLTETS ALFEDGTVEE DIDVIVFATG YTFSFPFLEE SLVKIEHNMV SLYKYMFPPQ
LEKPTLTCMG LIQPLGSIFP TVELQARWAT RVFKGLCHLP SEKTMMEDII KRNEKRIDLF
GESQSQIVQT NYVDYLDELA LEIGAKPDLI SFLLKDPELA VKLCFGPCNS YQYRLVGPGQ
WEGARRAILT QKQRILKPLK TRSVKAAPNL SASFLMKILA LVAVFVAFFS QLYGF
