ID   SSUD_SHIF8              Reviewed;         381 AA.
AC   Q0T6A4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Alkanesulfonate monooxygenase;
DE            EC=1.14.14.5;
DE   AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase;
GN   Name=ssuD; OrderedLocusNames=SFV_0939;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z.,
RA   Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y.,
RA   Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000266; ABF03161.1; -; Genomic_DNA.
DR   RefSeq; YP_688466.1; -.
DR   SMR; Q0T6A4; 1-362.
DR   GeneID; 4208570; -.
DR   GenomeReviews; CP000266_GR; SFV_0939.
DR   KEGG; sfv:SFV_0939; -.
DR   HOGENOM; Q0T6A4; -.
DR   OMA; Q0T6A4; NIFWFLP.
DR   BioCyc; SFLE373384:SFV_0939-MON; -.
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; IPR011251; Luciferase-like.
DR   InterPro; IPR016048; Luciferase-like_sub.
DR   Gene3D; G3DSA:3.20.20.30; Luciferase_like; 1.
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   CHAIN         1    381       Alkanesulfonate monooxygenase.
FT                                /FTId=PRO_1000066836.
SQ   SEQUENCE   381 AA;  41671 MW;  5420A8AC75326BD1 CRC64;
     MSLNMFWFLP THGDGHYLGT EEGSRPVDHG YLQQIAQAAD RLGYTGVLIP TGRSCEDAWL
     VAASMIPVTQ RLKFLVALRP SVTSPTVAAR QAATLDRLSN GRALFNLVTG SDPQELAGDG
     VFLDHSERYE ASAEFTQVWR RLLLGETVNF NGKHSHVRGA KLLFPPIQQP YPPLYFGGSS
     DVAQELAAEQ VDLYLTWGEP PELVKEKIEQ VRAKAAAYGR KIRFGIRLHV IVRETNDEAW
     QAAERLISHL DDETIAKAQA AFARTDSVGQ QRMAALHNGK RDNLEISPNL WAGVGLVRGG
     AGTALVGDGP TVAARINEYA ALGIDSFVLS GYPHLEEAYR VGELLFPHLD VAIPEIPQPQ
     PLNPQGEAVA NDFIPRKVAQ S
//