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Database: UniProt
Entry: W5KC61_ASTMX
LinkDB: W5KC61_ASTMX
Original site: W5KC61_ASTMX 
ID   W5KC61_ASTMX            Unreviewed;       562 AA.
AC   W5KC61;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000005172.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000005172.2}
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|PIRNR:PIRNR000332, ECO:0000256|RuleBase:RU361177};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|PIRNR:PIRNR000332}.
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   AlphaFoldDB; W5KC61; -.
DR   STRING; 7994.ENSAMXP00000005172; -.
DR   Ensembl; ENSAMXT00000005172.2; ENSAMXP00000005172.2; ENSAMXG00000005049.2.
DR   eggNOG; KOG1399; Eukaryota.
DR   GeneTree; ENSGT00940000160836; -.
DR   HOGENOM; CLU_006909_8_2_1; -.
DR   InParanoid; W5KC61; -.
DR   OrthoDB; 2079054at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000005049; Expressed in mesonephros and 10 other cell types or tissues.
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:0034899; F:trimethylamine monooxygenase activity; IEA:RHEA.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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:SF204; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
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   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}; Membrane {ECO:0000256|PIRNR:PIRNR000332};
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:UP000018467}.
SQ   SEQUENCE   562 AA;  62857 MW;  9EDE132A7A5DAA4D CRC64;
     MARRVAVIGA GNAGLTCIKC CLDEGLEPVC FESSDDIGGL WRFKETPEAE CASIYRSLVV
     NTSKEMMCFS DFPMPAHYPN YMPHTLLLQY FRLYAEHFNL LKHIQLQTKV LSVKQRDDFS
     SSGQWEVVTE SRDGHKETQV FDGVLICSGH FSHPVTPLSA FPGIDTFPGK YIHSWEYKDP
     DPFRGQRVVV VGIGNSGVDI AVEISRVAEK TFLSTREGGW VVGRMAGSGL PLDIMVNRRF
     LAMLLRLPPR SLVNWAAERS YNKKYDHRLY ALQPNYRILD RRPIINDDLP GRIIQGALQI
     KPNIQQFRGS SVVFDNGVVE EGIDAVVFCT GYKATFPYLS PSIYSGPEGG MSLYNKVFPL
     SLEHPTLAII GLLNATGSLM PVAEMQARWA TRVIAGLNHL PPLATMQKMI GKEMKAKIKR
     YGSVKKAALE VDYIPYMDSI AQEVGVRPNL LYLFLTDPGL GWRVLYGPCT PFQYRLRGPG
     RWTGARQAIF TQWERVVQPL KTRPIPEPNI SGPSFWSLTG GAAVIFAIIV LQKSVPVFLQ
     DRVASIASLM TYIESVLGWR NV
//
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