ID   SSUD_ECOHS              Reviewed;         381 AA.
AC   A7ZYN8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
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=EcHS_A1044;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
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; CP000802; ABV05392.1; -; Genomic_DNA.
DR   RefSeq; WP_000056006.1; NC_009800.1.
DR   AlphaFoldDB; A7ZYN8; -.
DR   SMR; A7ZYN8; -.
DR   KEGG; ecx:EcHS_A1044; -.
DR   HOGENOM; CLU_027853_1_0_6; -.
DR   Proteomes; UP000001123; Chromosome.
DR   GO; GO:0008726; F:alkanesulfonate monooxygenase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01094; Alkanesulfonate_monoxygenase; 1.
DR   Gene3D; 3.20.20.30; Luciferase-like domain; 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   NCBIfam; TIGR03565; alk_sulf_monoox; 1.
DR   PANTHER; PTHR42847; ALKANESULFONATE MONOOXYGENASE; 1.
DR   PANTHER; PTHR42847:SF4; ALKANESULFONATE MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   SUPFAM; SSF51679; Bacterial luciferase-like; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..381
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_1000066820"
SQ   SEQUENCE   381 AA;  41736 MW;  4D05E510487999C6 CRC64;
     MSLNMFWFLP THGDGHYLGT EEGSRPVDHG YLQQIAQAAD RLGYTGVLIP TGRSCEDAWL
     VAASMIPVTQ RLKFLVALRP SVTSPTVAAR QAATLDRLSN GRALFNLVTG SDPQELAGDG
     VFLDHSERYE ASAEFTQVWR RLLQRETVDF NGKHIHVRGA KLLFPAIQQP YPPLYFGGSS
     DVAQELAAEQ VDLYLTWGEP PELVKEKIEQ VRAKAAAHGR KIRFGIRLHV IVRETNDEAW
     QAAERLISHL DDETIAKAQA AFARTDSVGQ QRMAALHNGK RDNLEISPNL WAGVGLVRGG
     AGTALVGDGP TVAARINEYA ALGIDSFVLS GYPHLEEAYR VGELLFPLLD VAIPEIPQPQ
     PLNPQGEAVA NDFIPRKVAQ S
//