ID G3RKD7_GORGO Unreviewed; 532 AA.
AC G3RKD7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 71.
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=FMO3 {ECO:0000313|Ensembl:ENSGGOP00000016202.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000016202.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000016202.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000016202.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000016202.3}
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}.
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DR EMBL; CABD030007242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030007243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004027936.1; XM_004027887.2.
DR RefSeq; XP_004027937.1; XM_004027888.2.
DR AlphaFoldDB; G3RKD7; -.
DR STRING; 9593.ENSGGOP00000016202; -.
DR Ensembl; ENSGGOT00000016661.3; ENSGGOP00000016202.3; ENSGGOG00000016607.3.
DR GeneID; 101125254; -.
DR KEGG; ggo:101125254; -.
DR CTD; 2328; -.
DR eggNOG; KOG1399; Eukaryota.
DR GeneTree; ENSGT00940000161339; -.
DR HOGENOM; CLU_006909_8_2_1; -.
DR InParanoid; G3RKD7; -.
DR OMA; DCYERET; -.
DR OrthoDB; 2079054at2759; -.
DR TreeFam; TF105285; -.
DR Proteomes; UP000001519; Chromosome 1.
DR Bgee; ENSGGOG00000016607; Expressed in liver.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047638; F:albendazole monooxygenase activity; IEA:RHEA.
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; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0034899; F:trimethylamine monooxygenase activity; IEA:RHEA.
DR GO; GO:0042412; P:taurine biosynthetic process; IEA:Ensembl.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 4.
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 3: Inferred from homology;
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:UP000001519};
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; 59999 MW; 012C0F9673E58A76 CRC64;
MGKKVAIIGA GVSGLASIRS CLEEGLEPTC FEKSNDIGGL WKFSDHAEEG RASIYKSVFS
NSSKEMMCFP DFPFPDDFPS FMHNSKIQEY IIAFAKEKNL LKYIQFKTFV SSVNKRPDFA
TSGQWDVTTE RDGKKESAVF DAVMVCSGHH VYPNLPKESF PGLNHFKGKC FHSRDYKEPG
VFNGKRVLVV GLGNSGCDIA TELSRTAEQV MISSRSGSWV MSRVWDNGYP WDMLLVTRFG
TFLKNNLPTA ISDWLYVKQM NARFKHENYG LMPLNGVLRK EPVFNDELPA CILCGIVSVK
PNVKEFTETS AIFEDGTIFE GIDCVIFATG YSFAYPFLDE SIIKSRNNEI ILFKGVFPPL
LEKSTIAVIG FVQSLGAAIP TADLQSRWAA QVIKGTCTLP SMEDMMNDIN EKMEKKRKWF
GKSETIQTDY IVYMDELSSF IGAKPNIPWL FLTDPKLAME VYFGPCSPYQ FRLVGPGQWP
GARNAILTQW DRSLKPMQTR VVGRLQKPCF FFHWLKLFAI PILLIAVFLV LT
//
