ID   SFNG_PSEPU              Reviewed;         363 AA.
AC   Q65YW9;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=FMNH(2)-dependent dimethylsulfone monooxygenase {ECO:0000303|PubMed:15661012};
DE            EC=1.14.14.35 {ECO:0000269|PubMed:15661012};
GN   Name=sfnG {ECO:0000303|PubMed:15661012};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DS1 {ECO:0000312|EMBL:BAD51730.1};
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]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DS1 {ECO:0000312|EMBL:BAD51730.1};
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 (Mosc.) 149:991-1000(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP   PHENOTYPE, AND INDUCTION.
RC   STRAIN=DS1 {ECO:0000312|EMBL:BAD51730.1};
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       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:15661012}.
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:15661012};
CC   -!- INDUCTION: Transcriptionally activated by SfnR.
CC       {ECO:0000269|PubMed:15661012}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC       dimethyl sulfide (DMS), dimethylsulfone (DMSO2) and diethyl sulphone
CC       (DESO2). {ECO:0000269|PubMed:15661012}.
CC   -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000305}.
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DR   EMBL; AB174850; BAD51730.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q65YW9; -.
DR   SMR; Q65YW9; -.
DR   BioCyc; MetaCyc:MON-14251; -.
DR   BRENDA; 1.14.14.35; 5092.
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..363
FT                   /note="FMNH(2)-dependent dimethylsulfone monooxygenase"
FT                   /id="PRO_0000443538"
SQ   SEQUENCE   363 AA;  40268 MW;  CA9E6AF32B0DDA2F CRC64;
     MSQPIKFAYW VPNVSGGLVV SKIEQRTSWD IDYNRKLAQI AERSGFEYAL SQIRFTAGYG
     ADNQHESVTI SHALLAATEK LKVIAAILPG PWSPALAAKQ LATIDQFTGG RIAVNVVSGW
     FKGEFRAIGE PWLEHDERYR RSEEFIRALK GIWTQDNFSF HGDFYRFNDY TLKPKPLQRP
     HPEIFQGGSS RAARDMASRV SDWYFTNGNS VEGIKAQVDD IRAKAAANGH AVKIGVNAFV
     IARDTEEEAR AVLAEIIAKA DPEAVNGFGS EVKNAGAASP EGEGNWAKST FEDLVQYNDG
     FKTNLIGTPR QIAERIVALK AIGVDLILSG FLHFQEEVEY FGRHVLPLVR ELEQERRAAV
     AVA