ID   SSUD_ECOL6              Reviewed;         381 AA.
AC   Q8FJ93;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Alkanesulfonate monooxygenase;
DE            EC=1.14.14.5;
DE   AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase;
GN   Name=ssuD; Synonyms=ycbN; OrderedLocusNames=c1078;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: An alkanesufonate (R-CH(2)-SO(3)H) + FMNH(2) +
CC       O(2) = an aldehyde (R-CHO) + FMN + sulfite + H(2)O.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- MISCELLANEOUS: FMNH(2) which is absolutely required for this
CC       enzymatic reaction, is provided by ssuE (By similarity).
CC   -!- SIMILARITY: Belongs to the ssuD family.
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DR   EMBL; AE014075; AAN79546.1; -; Genomic_DNA.
DR   RefSeq; NP_753003.1; -.
DR   HSSP; P80645; 1M41.
DR   SMR; Q8FJ93; 1-362.
DR   GeneID; 1038862; -.
DR   GenomeReviews; AE014075_GR; c1078.
DR   KEGG; ecc:c1078; -.
DR   NMPDR; fig|199310.1.peg.1046; -.
DR   HOGENOM; Q8FJ93; -.
DR   OMA; Q8FJ93; NIFWFLP.
DR   BRENDA; 1.14.14.5; 292881.
DR   GO; GO:0008726; F:alkanesulfonate monooxygenase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01229; -; 1.
DR   InterPro; IPR019911; Alkanesulfonate_mOase_FMN-dep.
DR   InterPro; IPR016048; Luciferase-like_sub.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   TIGRFAMs; TIGR03565; Alk_sulf_monoox; 1.
PE   3: Inferred from homology;
KW   Complete proteome; FMN; Monooxygenase; Oxidoreductase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    381       Alkanesulfonate monooxygenase.
FT                                /FTId=PRO_0000216707.
SQ   SEQUENCE   381 AA;  41686 MW;  6C12DE4275E9C7A9 CRC64;
     MSLNMFWFLP THGDGHYLGT EEGSRPIDHG YLQQIAQAAD RLGYTGVLIP TGRSCEDAWL
     VAASMIPVTQ RLKFLVALRP SVTSPTVAAR QAATLDRLSN GRALFNLVTG SDPQELAGDG
     VFLDHSERYE ASAEFTQVWR RLLLGETVDF NGKHIHVRGA KLLFPPIQQP YPPLYFGGSS
     DVAQELAAEQ VDLYLTWGEP PELVKEKIEH VRAKAAAHGR KIRFGVRLHV IVRETNDEAW
     QAAERLISRL DDETIAKAQA AFARTDSVGQ QRMAALHNGK RDNLEISPNL WAGVGLVRGG
     AGTALVGDGP TVAARINEYA ALGIDSFVLS GYPHLEEAYR VGELLFPHLD VAIPEIPQPQ
     PLNPQGEAVA NDFIPRNVAQ S
//