ID   SSUD_ERWP6              Reviewed;         383 AA.
AC   D2TDP0;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   25-MAY-2022, entry version 49.
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=EPYR_02427;
OS   Erwinia pyrifoliae (strain DSM 12163 / CIP 106111 / Ep16/96).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=644651;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12163 / CIP 106111 / Ep16/96;
RX   PubMed=20047678; DOI=10.1186/1471-2164-11-2;
RA   Smits T.H., Jaenicke S., Rezzonico F., Kamber T., Goesmann A., Frey J.E.,
RA   Duffy B.;
RT   "Complete genome sequence of the fire blight pathogen Erwinia pyrifoliae
RT   DSM 12163T and comparative genomic insights into plant pathogenicity.";
RL   BMC Genomics 11:2-2(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAY74807.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; FN392235; CAY74807.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_012668534.1; NC_017390.1.
DR   AlphaFoldDB; D2TDP0; -.
DR   SMR; D2TDP0; -.
DR   EnsemblBacteria; CAY74807; CAY74807; EPYR_02427.
DR   KEGG; epr:EPYR_02427; -.
DR   PATRIC; fig|644651.3.peg.2216; -.
DR   HOGENOM; CLU_027853_1_0_6; -.
DR   Proteomes; UP000008690; 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..383
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_0000403215"
SQ   SEQUENCE   383 AA;  41859 MW;  9275C5D0A3171679 CRC64;
     MRLSVFWFLP THGDGKYLGT NEGARPVDHA YLQQIAQAAD RLGFGGVLIP TGRSCEDAWL
     VAASLIPVTQ RLRFLVALRP GVISPTQAAR QAATLDRLSN GRALFNLVTG GDAEELAGDG
     VFLDHGERYA ESAEFTRVWR RVLEGETVDY KGKHVHVRGA RLMFKPVQQP RPPLWFGGSS
     EVAQDLAAEQ VDVYLTWGEP PAQVKEKIAR VQAKAAARGR KVRFGIRLHV IVRETNDEAW
     QAADRLISHL DDQTIAKAQA ALARTDSVGQ QRMAALHGGK RDRLEISPNL WAGVGLVRGG
     AGTALVGDGP TVAARMQEYA DLGIETFILS GYPHLEEAYR VGELLFPHLE LNIPEVPKPA
     AVQAHGEHVA HDFAPQKVPQ GER