ID   SFNC_PSEPU              Reviewed;         395 AA.
AC   Q845S8;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Probable FMNH2-dependent monooxygenase SfnC {ECO:0000303|PubMed:12835925};
DE            EC=1.14.14.- {ECO:0000305};
GN   Name=sfnC {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].
RC   STRAIN=DS1 {ECO:0000312|EMBL:BAC66052.1};
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], FUNCTION, AND INDUCTION.
RC   STRAIN=DS1 {ECO:0000312|EMBL:BAC66052.1};
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).
CC   -!- FUNCTION: Involved in the dimethyl sulfide degradation pathway.
CC       {ECO:0000269|PubMed:12686641}.
CC   -!- INDUCTION: Under sulfate limitation conditions, it is transcriptionally
CC       activated by the LysR-type transcriptional regulator, CysB.
CC       {ECO:0000269|PubMed:12686641}.
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DR   EMBL; AB091764; BAC66052.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q845S8; -.
DR   SMR; Q845S8; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR013107; Acyl-CoA_DH_C.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   2: Evidence at transcript level;
KW   Flavoprotein; FMN; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..395
FT                   /note="Probable FMNH2-dependent monooxygenase SfnC"
FT                   /id="PRO_0000443539"
SQ   SEQUENCE   395 AA;  44071 MW;  BE9BC6E269594FB2 CRC64;
     MNAPVNTPPR PALAIARELA GQFAQTAVER DDRGGTPKAE RDALRDSGLL SLVIPQAFGG
     QGASWHDTFA VVREFARVDS SIAHVFGFHH LMLATVRLFS RPDQWQPWFE QTARKQWFWG
     NALNPLDTRT VVKHFDGWCE FSGKKSFCSG ASDSEMLIAS AVDERAGGKL LIAAIPSGRT
     GISLHNDWNN IGQRQTDSGS ATFERVRVEH NELLLDPGPL STPFAALRPL IAQLHFANLF
     LGIAEGAFEE ARQYTLKESR PWFRSSAASS AEDPYVLRHY GEFWVGLESV RLLIERAARQ
     LDAAWAKEHA LTAQERGDLA LAIGTAKVAA SRHGLDICNR LFEVTGARAT HASLRFDRHW
     RNLRTQTLHD PVDYRIHELG EWALNDKRPA PSFYS