ID   SFNG_PSEPF              Reviewed;         364 AA.
AC   Q3KC85;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=FMNH(2)-dependent dimethylsulfone monooxygenase {ECO:0000303|PubMed:27392454};
DE            EC=1.14.14.35 {ECO:0000269|PubMed:27392454};
GN   Name=sfnG {ECO:0000303|PubMed:27392454};
GN   OrderedLocusNames=Pfl01_2879 {ECO:0000312|EMBL:ABA74620.1};
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:ABA74620.1,
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, AND CATALYTIC ACTIVITY.
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 oxidation of dimethylsulfone (DMSO2) to yield
CC       methanesulfinate, which is oxidized spontaneously to methanesulfonate
CC       in the presence of dioxygen and FMNH(2). {ECO:0000269|PubMed:27392454}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethyl sulfone + FMNH2 + O2 = FMN + formaldehyde + 2 H(+) +
CC         H2O + methanesulfinate; Xref=Rhea:RHEA:50716, ChEBI:CHEBI:9349,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16842, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:133603; EC=1.14.14.35;
CC         Evidence={ECO:0000269|PubMed:27392454};
CC   -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000305}.
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DR   EMBL; CP000094; ABA74620.1; -; Genomic_DNA.
DR   RefSeq; WP_011334289.1; NC_007492.2.
DR   AlphaFoldDB; Q3KC85; -.
DR   SMR; Q3KC85; -.
DR   STRING; 205922.Pfl01_2879; -.
DR   EnsemblBacteria; ABA74620; ABA74620; Pfl01_2879.
DR   KEGG; pfo:Pfl01_2879; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_2_6; -.
DR   OMA; ILPGPWN; -.
DR   BioCyc; MetaCyc:MON-20055; -.
DR   BRENDA; 1.14.14.35; 5121.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 3.20.20.30; -; 1.
DR   InterPro; IPR024014; DMSO2_SphG.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   SUPFAM; SSF51679; SSF51679; 1.
DR   TIGRFAMs; TIGR04021; LLM_DMSO2_sfnG; 1.
PE   1: Evidence at protein level;
KW   Flavoprotein; FMN; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..364
FT                   /note="FMNH(2)-dependent dimethylsulfone monooxygenase"
FT                   /id="PRO_0000443537"
SQ   SEQUENCE   364 AA;  40339 MW;  88E5440F60018D68 CRC64;
     MSQQAVKFAY WVPNVSGGLV VSRIEQRTDW GIDYNRKLAQ LAEAAGFEYA LTQIRFTAGY
     GAEFQHESVA FSHALLAATS QLKVIAAILP GPWQPALAAK QLATIDQLTN GRIAVNIVSG
     WFRGEFQAIG EHWLEHDERY RRSEEFIRSL RGIWSQDNFT FRGDFYRFDN YSLKPKPLGR
     PEIFQGGSSR AARDMAARVS DWYFTNGNSV EGIKAQVDDI RAKAAANHHS VKIGVNAFVI
     ARDTEEEAKA VLAQIIDQAD PEAVNAFGDA AKQAGRASPE GEGNWAKSTF EDLVQYNDGF
     KTNLIGTPQQ IAERIVALKA VGVDLVLAGF LHFQEEVEYF GQRVLPLVRE LEAKAQSART
     AEVA