ID   SSUD_ECO24              Reviewed;         381 AA.
AC   A7ZK27;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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};
GN   OrderedLocusNames=EcE24377A_1037;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV16534.1; -; Genomic_DNA.
DR   RefSeq; WP_000055996.1; NC_009801.1.
DR   AlphaFoldDB; A7ZK27; -.
DR   SMR; A7ZK27; -.
DR   EnsemblBacteria; ABV16534; ABV16534; EcE24377A_1037.
DR   GeneID; 66670789; -.
DR   KEGG; ecw:EcE24377A_1037; -.
DR   HOGENOM; CLU_027853_1_0_6; -.
DR   OMA; NIFWFLP; -.
DR   Proteomes; UP000001122; 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_1000066819"
SQ   SEQUENCE   381 AA;  41671 MW;  09146AD3B36BE936 CRC64;
     MSLNMFWFLP THGDGHYLGT EEGSRPVDHG YLQQIAQAAD RLGYTGVLIP TGRSCEDAWL
     VAASMIPVTQ RLKFLVALRP SVTSPTVAAR QAATLDRLSN GRALFNLVTG SDPQELAGDG
     VFLDHSERYE ASAEFTQVWR RLLLGETVNF NGKHIHVRGA KLLFPPIQQP YPPLYFGGSS
     DVAQELAAEQ VDLYLTWGEP PELVKEKIEQ VRAKAAAHGR KIRFGIRLHV IVRETNDEAW
     QAAERLISHL DDETIAKAQA AFARTDSVGQ QRMAALHNGK RDNLEISPNL WAGVGLVRGG
     AGTALVGDGP TVAARINEYA ALGIDSFVLS GYPHLEEAYR VGELLFPHLD VAIPEIPQPQ
     PLNPQGEAVA NDFIPRKVAQ S