ID   SSUD_RHOPT              Reviewed;         391 AA.
AC   B3QIN8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Rpal_2883;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001096; ACF01391.1; -; Genomic_DNA.
DR   RefSeq; WP_012496054.1; NC_011004.1.
DR   AlphaFoldDB; B3QIN8; -.
DR   SMR; B3QIN8; -.
DR   EnsemblBacteria; ACF01391; ACF01391; Rpal_2883.
DR   KEGG; rpt:Rpal_2883; -.
DR   HOGENOM; CLU_027853_1_0_5; -.
DR   OMA; YGFWLPI; -.
DR   OrthoDB; 919913at2; -.
DR   BioCyc; RPAL395960:RPAL_RS14290-MON; -.
DR   Proteomes; UP000001725; 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.
FT   CHAIN           1..391
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_1000139628"
SQ   SEQUENCE   391 AA;  42441 MW;  7E33810E3F585C79 CRC64;
     MTAPQTPSSN FLWFLPTHGD GHYLGTSNGG RDVNFGYLRQ IAQAADQLGY FGVLLPTGRS
     CEDSWVVASA VAPWTERLRY LVAVRPGLQS PSVAARMTAT LDRVIGGRLL VNVVTGGDPV
     ENKGDGVFLS HDERYEVTRE FLNVYSDLLS GKTVNVAGKH ITIEDGRLLF PPVQSPRPPL
     YFGGSSDAGI DVAADTVDKY LTWGEPPAQV AEKVNRVRAV AEQRGRKLSF GIRLHVIVRE
     TNEAAWAAAD DLIRYVTDDT IAAAQKVFAR MDSVGQQRMS ELHGGRRDKL EISPNLWAGV
     GLVRGGAGTA LVGDPQTVAA RIKEYQDVGI DTFILSGYPH LEEAYRFAEL VFPLVKSLHA
     GNVTPLRANT GPFGETIANE HLPNAKQAVK P