ID   SFNF_PSEPF              Reviewed;         187 AA.
AC   Q3K9A2;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=NADH-dependent FMN reductase SfnF {ECO:0000303|PubMed:27392454};
DE            EC=1.5.1.42 {ECO:0000269|PubMed:27392454};
DE   AltName: Full=NADH-flavin reductase {ECO:0000305|PubMed:27392454};
GN   Name=sfnF {ECO:0000305}; Synonyms=msuE {ECO:0000303|PubMed:27392454};
GN   OrderedLocusNames=Pfl01_3915 {ECO:0000312|EMBL:ABA75652.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000312|EMBL:ABA75652.1,
RC   ECO:0000312|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=27392454; DOI=10.1016/j.abb.2016.07.001;
RA   Wicht D.K.;
RT   "The reduced flavin-dependent monooxygenase SfnG converts dimethylsulfone
RT   to methanesulfinate.";
RL   Arch. Biochem. Biophys. 604:159-166(2016).
CC   -!- FUNCTION: Involved in the dimethyl sulfide degradation pathway.
CC       Catalyzes the NADH-dependent reduction of FMN.
CC       {ECO:0000269|PubMed:27392454}.
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:0000269|PubMed:27392454};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8 uM for FMNH(2) {ECO:0000269|PubMed:27392454};
CC         KM=69 uM for NADH {ECO:0000269|PubMed:27392454};
CC         Vmax=37 umol/min/mg enzyme toward FMNH(2)
CC         {ECO:0000269|PubMed:27392454};
CC         Vmax=27 umol/min/mg enzyme toward NADH {ECO:0000269|PubMed:27392454};
CC         Note=kcat is 14 sec(-1) for FMNH(2) as substrate. kcat is 10 sec(-1)
CC         for NADH as substrate. {ECO:0000269|PubMed:27392454};
CC   -!- SIMILARITY: Belongs to the SsuE family. {ECO:0000305}.
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DR   EMBL; CP000094; ABA75652.1; -; Genomic_DNA.
DR   RefSeq; WP_011335230.1; NC_007492.2.
DR   AlphaFoldDB; Q3K9A2; -.
DR   SMR; Q3K9A2; -.
DR   STRING; 205922.Pfl01_3915; -.
DR   EnsemblBacteria; ABA75652; ABA75652; Pfl01_3915.
DR   KEGG; pfo:Pfl01_3915; -.
DR   eggNOG; COG0431; Bacteria.
DR   HOGENOM; CLU_055322_3_3_6; -.
DR   OMA; FMSHTLP; -.
DR   Proteomes; UP000002704; Chromosome.
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..187
FT                   /note="NADH-dependent FMN reductase SfnF"
FT                   /id="PRO_0000443540"
SQ   SEQUENCE   187 AA;  20264 MW;  0E52E2097CE8E30E CRC64;
     MSRPLKVVAL SGGTWRPSRT LVLTQALLAE LSGHLPIESH LIELGDIARP LGAALSRQEL
     PAEIEAELQA IEQADLLIVA APVYRGSYPG LLKHLFDLID LNALIDTPVL LAATGGSERH
     ALVLDHQLRP LFSFFQAVTL PIGVYATEAD FADYQITSEP LKARIRLAAE RAAPLFGTHL
     KPLLKIA