ID   SSUD_ACIAC              Reviewed;         391 AA.
AC   A1TRM3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Aave_3044;
OS   Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-2006) 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; CP000512; ABM33611.1; -; Genomic_DNA.
DR   RefSeq; WP_011796121.1; NC_008752.1.
DR   AlphaFoldDB; A1TRM3; -.
DR   SMR; A1TRM3; -.
DR   STRING; 397945.Aave_3044; -.
DR   EnsemblBacteria; ABM33611; ABM33611; Aave_3044.
DR   KEGG; aav:Aave_3044; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_0_4; -.
DR   OMA; NIFWFLP; -.
DR   OrthoDB; 919913at2; -.
DR   Proteomes; UP000002596; 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..391
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_1000066815"
SQ   SEQUENCE   391 AA;  42529 MW;  319746F760E3AE68 CRC64;
     MHVFWFIPTH GDSRYLGTSE GARAVHYDYL RQVATAADTL GYEGVLIPTG RSCEDPWVVA
     SALAPVTRRL KFLVAVRPGL HQPALAARMA ATFDRLSGGR LLINLVTGGD RTELEGDGVF
     LDHAQRYAQS EEFIRIWREI LSRSHEGGTF DYEGEHLSVK GAKLLYPPVQ KPYPPVYFGG
     SSEAAHDLAA EQVDTYLTWG EPPAAVAQKV ADVRARAAQR GRTVRFGIRL HVIVRETDAA
     AWAAAEELIS RVQDETVAQA QAVFSRMDSE GQRRMAALHA GGTRRSRADL EISPNLWAGV
     GLVRGGAGTA LVGDPQTVAA RMQEYADLGI DTFVLSGYPH LEEAYRFAEL VFPLLPAEVR
     ERIGGGRAAG PLTGPFGEIV GNQYVPRAAQ S