UniProt: A8WXJ0

Database: UniProt
Entry: A8WXJ0_CAEBR

LinkDB:  A8WXJ0_CAEBR 
Original site:  A8WXJ0_CAEBR

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Ontology (7)   
   GO (7)   
Gene (3)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   WORMBASE (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (4)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (18)   

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ID   A8WXJ0_CAEBR            Unreviewed;       500 AA.
AC   A8WXJ0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE            EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN   Name=fmo-1 {ECO:0000313|WormBase:CBG04431};
GN   ORFNames=CBG04431 {ECO:0000313|EMBL:CAP25130.1,
GN   ECO:0000313|WormBase:CBG04431}, CBG_04431
GN   {ECO:0000313|EMBL:CAP25130.1};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP25130.1, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP25130.1, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP25130.1,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranial + H(+) + NADPH + O2 = (1E)-2,6-
CC         dimethylhepta-1,5-dien-1-yl formate + H2O + NADP(+);
CC         Xref=Rhea:RHEA:54860, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16980, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:138375;
CC         Evidence={ECO:0000256|ARBA:ARBA00023916};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54861;
CC         Evidence={ECO:0000256|ARBA:ARBA00023916};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 + octan-3-one = H2O + NADP(+) + pentyl
CC         propanoate; Xref=Rhea:RHEA:54840, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:80946, ChEBI:CHEBI:87373;
CC         Evidence={ECO:0000256|ARBA:ARBA00001029};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54841;
CC         Evidence={ECO:0000256|ARBA:ARBA00001029};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 + octan-3-one = ethyl hexanoate + H2O +
CC         NADP(+); Xref=Rhea:RHEA:54856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:80946, ChEBI:CHEBI:86055;
CC         Evidence={ECO:0000256|ARBA:ARBA00001105};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54857;
CC         Evidence={ECO:0000256|ARBA:ARBA00001105};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 + sulcatone = 4-methylpent-3-en-1-yl acetate
CC         + H2O + NADP(+); Xref=Rhea:RHEA:54864, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16310,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:138373;
CC         Evidence={ECO:0000256|ARBA:ARBA00000299};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54865;
CC         Evidence={ECO:0000256|ARBA:ARBA00000299};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000458};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11261;
CC         Evidence={ECO:0000256|ARBA:ARBA00000458};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + heptan-2-one + NADPH + O2 = H2O + NADP(+) + pentyl
CC         acetate; Xref=Rhea:RHEA:54836, ChEBI:CHEBI:5672, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:87362;
CC         Evidence={ECO:0000256|ARBA:ARBA00000019};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54837;
CC         Evidence={ECO:0000256|ARBA:ARBA00000019};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + heptan-4-one + NADPH + O2 = H2O + NADP(+) + propyl
CC         butanoate; Xref=Rhea:RHEA:54852, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:89484, ChEBI:CHEBI:89719;
CC         Evidence={ECO:0000256|ARBA:ARBA00001839};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54853;
CC         Evidence={ECO:0000256|ARBA:ARBA00001839};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexan-3-one + NADPH + O2 = H2O + NADP(+) + propyl
CC         propanoate; Xref=Rhea:RHEA:54848, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:89828, ChEBI:CHEBI:89891;
CC         Evidence={ECO:0000256|ARBA:ARBA00000279};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54849;
CC         Evidence={ECO:0000256|ARBA:ARBA00000279};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexan-3-one + NADPH + O2 = ethyl butanoate + H2O +
CC         NADP(+); Xref=Rhea:RHEA:54844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:88764, ChEBI:CHEBI:89891;
CC         Evidence={ECO:0000256|ARBA:ARBA00000531};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54845;
CC         Evidence={ECO:0000256|ARBA:ARBA00000531};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU361177};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}. Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004524}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC       ECO:0000256|RuleBase:RU361177}.
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DR   EMBL; HE601251; CAP25130.1; -; Genomic_DNA.
DR   RefSeq; XP_002634420.1; XM_002634374.1.
DR   AlphaFoldDB; A8WXJ0; -.
DR   STRING; 6238.A8WXJ0; -.
DR   GeneID; 8576415; -.
DR   KEGG; cbr:CBG_04431; -.
DR   CTD; 8576415; -.
DR   WormBase; CBG04431; CBP49502; WBGene00027099; Cbr-fmo-1.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_545413_0_0_1; -.
DR   InParanoid; A8WXJ0; -.
DR   OMA; KREMMEN; -.
DR   OrthoDB; 2079054at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
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-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0106294; F:NADPH oxidase H202-forming activity; IEA:RHEA.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; IPR002257; Flavin_mOase_5.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF85; DIMETHYLANILINE MONOOXYGENASE [N-OXIDE-FORMING]; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01125; FMOXYGENASE5.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU361177};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361177};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549}.
SQ   SEQUENCE   500 AA;  57579 MW;  95800301C3C7B063 CRC64;
     MYCRICSDRS IPKPSTLSSI VWIPVQDIKN LSIDEILDHR GYEDKTVVVI GIGNSGGDVA
     VELSRIAKQV YLVTRRGTWV FNRIFDYGKP IDMVMNRKWI SDIRARVPEW LSNSVVEMKL
     NMRFDHQAYG LKPAHRVFGA HPTVNDELPN RIACGTVRIK PNIANFTEHG VVFEDGSKLD
     QVDEVVMSTG FSFEFNLVEE GKLIQVQDNH VSLYQYMFPT DLADQNTLAV IGLVQPFGSI
     MPLSEMQARV YLEQFTGNNV IPSKREMMEN VHDKLSKMAS RYVTSKRHTI QVDYVDYIEE
     LAKMIGAQLD MKKLWKEDPW LAYKVYFGPR VPYIYRLNGP HKWKEARDAI MSVDERVLMA
     TNDHAQVAPD YTVLYFADWY GKRRKTTTMK NGLNNSRERL MNHGEKNREC SRGFINGKLE
     QKFIQETCDE GMLYCIESYT GDFDEVTASC QHLGTNMRLL DLCQSKNPKK INEDLTTRCC
     KTDLCNNIGV EKKKLKKIEN
//

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