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FMO3_MACMU
ID   FMO3_MACMU              Reviewed;         532 AA.
AC   Q8SPQ7;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 3;
DE            EC=1.14.13.8 {ECO:0000250|UniProtKB:P31513};
DE            EC=1.14.14.73 {ECO:0000250|UniProtKB:P31513};
DE   AltName: Full=Dimethylaniline oxidase 3;
DE   AltName: Full=Hepatic flavin-containing monooxygenase 3;
DE            Short=FMO 3;
DE   AltName: Full=Trimethylamine monooxygenase;
DE            EC=1.14.13.148;
GN   Name=FMO3;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=11717182;
RA   Cashman J.R., Zhang J., Leushner J., Braun A.;
RT   "Population distribution of human flavin-containing monooxygenase form 3:
RT   gene polymorphisms.";
RL   Drug Metab. Dispos. 29:1629-1637(2001).
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:0000250|UniProtKB:P31513,
CC       ECO:0000250|UniProtKB:P97501}.
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:0000250|UniProtKB:P31513};
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:0000250|UniProtKB:P31513};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=fenbendazole + O2 + reduced [NADPH--hemoprotein reductase] =
CC         fenbendazole S-oxide + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:55928, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:35812, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:77092; EC=1.14.14.73;
CC         Evidence={ECO:0000250|UniProtKB:P31513};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=albendazole + O2 + reduced [NADPH--hemoprotein reductase] =
CC         albendazole S-oxide + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:55924, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16664, ChEBI:CHEBI:16959, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; EC=1.14.14.73;
CC         Evidence={ECO:0000250|UniProtKB:P31513};
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:0000250|UniProtKB:P31513};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane
CC       {ECO:0000250|UniProtKB:P32417}; Single-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P32417}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Liver.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR   EMBL; AY063498; AAL86612.1; -; mRNA.
DR   RefSeq; NP_001028065.1; NM_001032893.1.
DR   AlphaFoldDB; Q8SPQ7; -.
DR   SMR; Q8SPQ7; -.
DR   STRING; 9544.ENSMMUP00000010434; -.
DR   GeneID; 574244; -.
DR   KEGG; mcc:574244; -.
DR   CTD; 2328; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   InParanoid; Q8SPQ7; -.
DR   OrthoDB; 405736at2759; -.
DR   Proteomes; UP000006718; Unplaced.
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: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:0034899; F:trimethylamine monooxygenase activity; IEA:UniProtKB-EC.
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; IPR002255; Flavin_mOase_3.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01123; FMOXYGENASE3.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome;
KW   Monooxygenase; NADP; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..532
FT                   /note="Dimethylaniline monooxygenase [N-oxide-forming] 3"
FT                   /id="PRO_0000147655"
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         401
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97501"
SQ   SEQUENCE   532 AA;  60152 MW;  73A4D13EE2A24A72 CRC64;
     MGKKVAIIGA GVSGLASIRS CLEEGLEPTC FEKSNDIGGL WKFSDHAEEG RASIYKSVFT
     NSSKEMMCFP DFPYPDDFPN FMHNSKIQEY LTAFAKEKSL LKYIQFKTFV SSVNKRPDFA
     TTGQWDVTTE RDGKRESAVF DAVMVCSGHH VYPNLPKESF PGLNHFKGKC FHSRDYKEPG
     VFKGKRVLVV GLGNSGCDIA TELSHTAEQV VISSRSGSWV MSRVWDNGYP WDMVLITRFG
     TFLKNNLPTA ISDWLYMKQM NARFKHENYG LMPLNGVLRK EPVFNDELPA CILCGIVSVK
     PNVKKFTETS AIFEDGTTFE GIDCVIFATG YSYTYTFLDE SIIKNRNNEI ILFKGVFPPL
     LEKSTIAVIG FVQSLGAAIP TVDLQSRWAA RVIKGTCTLP SMEDMMNDIN EKMERKHKWY
     GKSETLQTDY IVYMDELSSF IGVKPNIPWL FLTDPKLAME VYFGPCSPYQ FRLVGPGKWP
     GARNAILTQW DRSLKPLQTR VVGRLQKPCF FFHWLKPFAI PILLIAVFLG LT
 
 
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