ID   SFNE_PSEPU              Reviewed;         186 AA.
AC   Q845S9;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=NADH-dependent FMN reductase SfnE {ECO:0000303|PubMed:12835925};
DE            EC=1.5.1.42 {ECO:0000305|PubMed:12835925, ECO:0000305|PubMed:15661012};
GN   Name=sfnE {ECO:0000303|PubMed:12686641};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DS1 {ECO:0000312|EMBL:BAC66051.1};
RX   PubMed=12835925; DOI=10.1007/s00253-003-1233-7;
RA   Endoh T., Kasuga K., Horinouchi M., Yoshida T., Habe H., Nojiri H.,
RA   Omori T.;
RT   "Characterization and identification of genes essential for dimethyl
RT   sulfide utilization in Pseudomonas putida strain DS1.";
RL   Appl. Microbiol. Biotechnol. 62:83-91(2003).
RN   [2] {ECO:0000312|EMBL:BAC66051.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=DS1 {ECO:0000312|EMBL:BAC66051.1};
RX   PubMed=12686641; DOI=10.1099/mic.0.26031-0;
RA   Endoh T., Habe H., Yoshida T., Nojiri H., Omori T.;
RT   "A CysB-regulated and sigma54-dependent regulator, SfnR, is essential for
RT   dimethyl sulfone metabolism of Pseudomonas putida strain DS1.";
RL   Microbiology 149:991-1000(2003).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DS1;
RX   PubMed=15661012; DOI=10.1111/j.1365-2958.2004.04431.x;
RA   Endoh T., Habe H., Nojiri H., Yamane H., Omori T.;
RT   "The sigma54-dependent transcriptional activator SfnR regulates the
RT   expression of the Pseudomonas putida sfnFG operon responsible for dimethyl
RT   sulphone utilization.";
RL   Mol. Microbiol. 55:897-911(2005).
CC   -!- FUNCTION: Involved in the dimethyl sulfide degradation pathway
CC       (PubMed:12835925, PubMed:12686641). Catalyzes the NADH-dependent
CC       reduction of FMN (PubMed:12835925, PubMed:15661012).
CC       {ECO:0000269|PubMed:12686641, ECO:0000269|PubMed:12835925,
CC       ECO:0000269|PubMed:15661012}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + NAD(+) = FMN + 2 H(+) + NADH; Xref=Rhea:RHEA:21620,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58210; EC=1.5.1.42;
CC         Evidence={ECO:0000305|PubMed:12835925, ECO:0000305|PubMed:15661012};
CC   -!- INDUCTION: Under sulfate limitation conditions, it is transcriptionally
CC       activated by the LysR-type transcriptional regulator, CysB.
CC       {ECO:0000269|PubMed:12686641}.
CC   -!- SIMILARITY: Belongs to the SsuE family. {ECO:0000305}.
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DR   EMBL; AB091764; BAC66051.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q845S9; -.
DR   SMR; Q845S9; -.
DR   GO; GO:0052874; F:FMN reductase (NADH) activity; IEA:RHEA.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProt.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR005025; FMN_Rdtase-like.
DR   InterPro; IPR019912; FMN_Rdtase_MsuE-like.
DR   Pfam; PF03358; FMN_red; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   TIGRFAMs; TIGR03566; FMN_reduc_MsuE; 1.
PE   1: Evidence at protein level;
KW   Flavoprotein; FMN; NAD; Oxidoreductase.
FT   CHAIN           1..186
FT                   /note="NADH-dependent FMN reductase SfnE"
FT                   /id="PRO_0000443542"
SQ   SEQUENCE   186 AA;  20086 MW;  2027EE8246C4A34D CRC64;
     MSTPLNVVAL SGGTSRPSRT LALTEAILAE LAEHLHIKPH LIELGEIARP LGSALWRSEL
     PEAVEQQLRL VEKADLLVVT TPVYRGSFTG HFKHLFDLIG QDALVDTPVL LAATGGSERH
     ALVLDHQLRP LFSFLQALTL PIGVFASQAE MADYRVSSAA LAARIRLAAE RAVPLFGAHH
     ALRKSA