ID Q5REM1_PONAB Unreviewed; 532 AA.
AC Q5REM1; A0A2J8UBR9; A0A6D2WTK5; H2N4R1;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 3 {ECO:0000256|PIRNR:PIRNR000332};
DE EC=1.14.13.148 {ECO:0000256|PIRNR:PIRNR000332};
DE EC=1.14.13.32 {ECO:0000256|PIRNR:PIRNR000332};
DE EC=1.14.13.8 {ECO:0000256|PIRNR:PIRNR000332};
GN Name=DKFZp468G1222 {ECO:0000313|EMBL:CAH89786.1};
GN Synonyms=FMO3 {ECO:0000313|Ensembl:ENSPPYP00000000600.2};
GN ORFNames=CR201_G0028887 {ECO:0000313|EMBL:PNJ42693.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|EMBL:CAH89786.1};
RN [1] {ECO:0000313|EMBL:CAH89786.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Heart {ECO:0000313|EMBL:CAH89786.1};
RG The German cDNA Consortium;
RA Ottenwaelder B., Obermaier B., Deutschenbaur S., Schaipp A., Mewes H.W.,
RA Weil B., Amid C., Osanger A., Fobo G., Han M., Wiemann S.;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000000600.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PNJ42693.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ42693.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSPPYP00000000600.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Essential hepatic enzyme that catalyzes the oxygenation of a
CC wide variety of nitrogen- and sulfur-containing compounds including
CC drugs as well as dietary compounds. Plays an important role in the
CC metabolism of trimethylamine (TMA), via the production of
CC trimethylamine N-oxide (TMAO) metabolite. TMA is generated by the
CC action of gut microbiota using dietary precursors such as choline,
CC choline containing compounds, betaine or L-carnitine. By regulating
CC TMAO concentration, FMO3 directly impacts both platelet responsiveness
CC and rate of thrombus formation. {ECO:0000256|PIRNR:PIRNR000332}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-nicotine + NADPH + O2 = H2O + NADP(+) + trans-(S)-nicotine
CC N(1')-oxide; Xref=Rhea:RHEA:58720, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:59806, ChEBI:CHEBI:142660;
CC Evidence={ECO:0000256|ARBA:ARBA00036085};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58721;
CC Evidence={ECO:0000256|ARBA:ARBA00036085};
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:0000256|ARBA:ARBA00000700};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24469;
CC Evidence={ECO:0000256|ARBA:ARBA00000700};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hypotaurine + NADPH + O2 = H2O + NADP(+) + taurine;
CC Xref=Rhea:RHEA:69819, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:57853,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:507393; EC=1.14.13.8;
CC Evidence={ECO:0000256|ARBA:ARBA00034434};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69820;
CC Evidence={ECO:0000256|ARBA:ARBA00034434};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + O2 + trimethylamine = H2O + NADP(+) + trimethylamine
CC N-oxide; Xref=Rhea:RHEA:31979, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15724, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58389; EC=1.14.13.148;
CC Evidence={ECO:0000256|ARBA:ARBA00034415};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31980;
CC Evidence={ECO:0000256|ARBA:ARBA00034415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=albendazole + H(+) + NADPH + O2 = albendazole S-oxide + H2O +
CC NADP(+); Xref=Rhea:RHEA:10796, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16664, ChEBI:CHEBI:16959,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.32;
CC Evidence={ECO:0000256|ARBA:ARBA00036808};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10797;
CC Evidence={ECO:0000256|ARBA:ARBA00036808};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|RuleBase:RU361177};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Microsome membrane
CC {ECO:0000256|ARBA:ARBA00004111}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004111}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|RuleBase:RU361177}.
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; CR857503; CAH89786.1; -; mRNA.
DR EMBL; NDHI03003464; PNJ42693.1; -; Genomic_DNA.
DR RefSeq; NP_001124820.1; NM_001131348.1.
DR RefSeq; XP_009239260.1; XM_009240985.1.
DR STRING; 9601.ENSPPYP00000000601; -.
DR Ensembl; ENSPPYT00000000625.2; ENSPPYP00000000600.2; ENSPPYG00000000518.2.
DR GeneID; 100171678; -.
DR KEGG; pon:100171678; -.
DR CTD; 2328; -.
DR eggNOG; KOG1399; Eukaryota.
DR GeneTree; ENSGT00940000161339; -.
DR HOGENOM; CLU_006909_8_2_1; -.
DR OMA; DCYERET; -.
DR OrthoDB; 2079054at2759; -.
DR TreeFam; TF105285; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0047822; F:hypotaurine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0042412; P:taurine biosynthetic process; IEA:Ensembl.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR002255; Flavin_mOase_3.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF44; DIMETHYLANILINE MONOOXYGENASE [N-OXIDE-FORMING] 3; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01123; FMOXYGENASE3.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR000332};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000332};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000332};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000332};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|PIRNR:PIRNR000332};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000332};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000332};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 510..531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 532 AA; 60175 MW; 4E7E37292B5C627F CRC64;
MGKKVAIIGA GVSGLASIRS CLEEGLEPTC FEKSNDIGGL WKFSDHAEEG RASIYKSVFS
NSSKEMMCFP DFPFPDDFPN FMHNSKIQEY IIAFAKEKNL LKYIQFKTFV SSINKRPDFA
TTGQWDVTTE RDGKKESAVF DAVMVCSGHH VYPNLPKESF PGLNHFKGKC FHSRDYKEPG
VFNGKRVLVV GLGNSGCDIA TELSHTAEQV MISSRSGSWV MSRVWDNGYP WDMLLITRFG
TFLKNNLPTA ISDWLYVKQM NTRFKHENYG LMPLNGVLRK EPVFNDELPA CILCGIVSIK
PNVKEFTETS AIFEDGTIFE GIDCVIFATG YSFAYPFLDE SIIKSRNNEI ILFKGVFPPL
LEKSTIAVIG FVQSLGAAIP TVDLQSRWAA QVINGTCTLP SMEDMMNDIN EKMEKKRKWF
GKSETIQTDY IVYMDELSSF IGAKPNIPWL FLTDPKLAVE VYFGPCSPYQ FRLVGPGQWP
GARNAILTQW DRSLKPMQTR VVRRLQKPCF FFHWLKLFAI PILLIAVFLV LT
//
