ID   SSUD_ENT38              Reviewed;         381 AA.
AC   A4W8V4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-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=Ent638_1454;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(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   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01229}.
CC   -!- MISCELLANEOUS: FMNH(2) which is absolutely required for this enzymatic
CC       reaction, is provided by SsuE. {ECO:0000255|HAMAP-Rule:MF_01229}.
CC   -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01229}.
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DR   EMBL; CP000653; ABP60134.1; -; Genomic_DNA.
DR   RefSeq; WP_012016851.1; NC_009436.1.
DR   AlphaFoldDB; A4W8V4; -.
DR   SMR; A4W8V4; -.
DR   STRING; 399742.Ent638_1454; -.
DR   EnsemblBacteria; ABP60134; ABP60134; Ent638_1454.
DR   KEGG; ent:Ent638_1454; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_0_6; -.
DR   OMA; NIFWFLP; -.
DR   OrthoDB; 919913at2; -.
DR   Proteomes; UP000000230; 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..381
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_1000066824"
SQ   SEQUENCE   381 AA;  41795 MW;  B4691862C7A81F9B CRC64;
     MSLNLFWFLP THGDGHYLGT EEGARPVDYG YLQQIAQAAD RIGFTGVLIP TGRSCEDAWL
     VAAAMIPVTQ RLKFLVALRP SVVSPTVAAR QAATLDRLSN GRALFNLVTG SDPTELAGDG
     VFLDHTERYE ASAEFTRVWR RLLEGDTVTY EGKHIRVRDA KLYFPPVQQP RPPLYFGGSS
     DVAQDLAAEQ VDLYLTWGEP PEQVKEKIEQ VRAKAAAHGR KVRFGIRLHV IVRETNQEAW
     QAADRLISHL DDDTIAKAQA ALAKTDSVGQ HRMASLHNGK RENLEISPNL WAGVGLVRGG
     AGTALVGDGP TVAARINEYA DLGIDSFILS GYPHLEEAYN VGELLFPHLD VAIPEIPQPR
     PLQVQGEAVA NEFIPRKTAQ S