ID A0A2I3HBN2_NOMLE Unreviewed; 469 AA.
AC A0A2I3HBN2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN Name=FMO1 {ECO:0000313|Ensembl:ENSNLEP00000040912.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000040912.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000040912.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000040912.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 + NADH + O2 = H2O + NAD(+) + taurine;
CC Xref=Rhea:RHEA:74111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57853,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:507393; EC=1.14.13.8;
CC Evidence={ECO:0000256|ARBA:ARBA00034447};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74112;
CC Evidence={ECO:0000256|ARBA:ARBA00034447};
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361177};
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC ECO:0000256|RuleBase:RU361177}.
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DR EMBL; ADFV01184582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01184583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01184584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01184585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01184586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01184587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01184588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003258919.1; XM_003258871.2.
DR AlphaFoldDB; A0A2I3HBN2; -.
DR Ensembl; ENSNLET00000049063.1; ENSNLEP00000040912.1; ENSNLEG00000015160.2.
DR GeneID; 100590364; -.
DR CTD; 2326; -.
DR GeneTree; ENSGT00940000160945; -.
DR OrthoDB; 2079054at2759; -.
DR Proteomes; UP000001073; Chromosome 12.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
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-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0034899; F:trimethylamine monooxygenase activity; IEA:RHEA.
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; IPR002253; Flavin_mOase_1.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF154; DIMETHYLANILINE MONOOXYGENASE [N-OXIDE-FORMING] 1; 1.
DR Pfam; PF00743; FMO-like; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PIRSF; PIRSF000332; FMO; 2.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01121; FMOXYGENASE1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU361177};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361177}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU361177}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361177};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073}.
SQ SEQUENCE 469 AA; 52813 MW; E53E599C0ED4B83F CRC64;
MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTTKVCSV IKCSDFAVSG
QWEVVTMHEE KQESAIFDAV MVCTGFLTNP YLPLDSFPGI NAFKGQYFHS RQYKHPDIFK
DKRVLVIGMG NSGTDIAVEA SHLAEKVFLS TTGGGWVISR IFDSGYPWDM VFMTRFQNML
RNSLPTPIVT WLMARKINNW LNHANYGLIP EDRTQLKEFV LNDELPGRII TGKVFIRPSV
KEVKENSVIF NNTSKEEPID IIVFATGYTF AFPFLDESVV KVEDGQASLY KYIFPAHLQK
PTLAVIGLIK PLGSMIPTGE TQARWAVRVL KGVNKLPPPS VMIEEINARK ENKPSWFGLC
YCKALQSDYI TYIDELLTYI NAKPNLFSML LTDPHLALTV FFGPCSPYQF RLTGPGKWEG
ARNAIMTQWD RTFKVIKARV VQESPSPFES FLKLFSFLAL LVAIFLIFL
//
