ID   SSUD_CUPMC              Reviewed;         387 AA.
AC   Q1LNM2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Alkanesulfonate monooxygenase {ECO:0000255|HAMAP-Rule:MF_01229};
DE            EC=1.14.14.5 {ECO:0000255|HAMAP-Rule:MF_01229};
DE   AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase {ECO:0000255|HAMAP-Rule:MF_01229};
GN   Name=ssuD {ECO:0000255|HAMAP-Rule:MF_01229}; OrderedLocusNames=Rmet_1371;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
CC   -!- FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates.
CC       {ECO:0000255|HAMAP-Rule:MF_01229}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + 2 H(+) +
CC         H2O + sulfite; Xref=Rhea:RHEA:23064, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17359,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:134249; EC=1.14.14.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01229};
CC   -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01229}.
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DR   EMBL; CP000352; ABF08254.1; -; Genomic_DNA.
DR   RefSeq; WP_011516133.1; NC_007973.1.
DR   AlphaFoldDB; Q1LNM2; -.
DR   SMR; Q1LNM2; -.
DR   STRING; 266264.Rmet_1371; -.
DR   EnsemblBacteria; ABF08254; ABF08254; Rmet_1371.
DR   KEGG; rme:Rmet_1371; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_0_4; -.
DR   OMA; NIFWFLP; -.
DR   OrthoDB; 919913at2; -.
DR   Proteomes; UP000002429; Chromosome.
DR   GO; GO:0008726; F:alkanesulfonate monooxygenase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.30; -; 1.
DR   HAMAP; MF_01229; Alkanesulf_monooxygen; 1.
DR   InterPro; IPR019911; Alkanesulphonate_mOase_FMN-dep.
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; TIGR03565; alk_sulf_monoox; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..387
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_1000066834"
SQ   SEQUENCE   387 AA;  41844 MW;  E8B67249071A3DCC CRC64;
     MQVLWFIPTH GDSRYLGTSE GAREVSFDYL KQVAVAADTL GYDGVLIPTG RSCEDPWVVA
     SALAAVTRKL RFLVALRPGL MTPTLAARMA ATFDRVSNGR LLVNLVTGGD VAELEGDGLF
     LNHAERYEAS AEFIRVWRDL LAASHENGEI SFEGKHVTVK GARVLYPPIQ RPHPPVYFGG
     SSEAAHDLAA EQVETYLTWG EPPADVAKKI ADVRARAAKH GRTVRFGIRL HVIVRETDAA
     AWAAADELIS KLDDQTVARA QAVFAKMDSE GQRRMAALHA GGTRRTREAL EISPNLWAGV
     GLVRGGAGTA LVGDPKTVAA RIEEYAALGI DTFVLSGYPH LEEAYRFAEL VFPLLPRKVR
     DKLPGQVLSG PFGEVMATGI VPIASQS