ID SSUD_ECOL5 Reviewed; 381 AA. AC Q0TJB9; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=Alkanesulfonate monooxygenase; DE EC=1.14.14.5; DE AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase; GN Name=ssuD; OrderedLocusNames=ECP_0947; OS Escherichia coli O6:K15:H31 (strain 536 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=362663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x; RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.; RT "Role of pathogenicity island-associated integrases in the genome RT plasticity of uropathogenic Escherichia coli strain 536."; RL Mol. Microbiol. 61:584-595(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; CP000247; ABG68960.1; -; Genomic_DNA. DR RefSeq; YP_668861.1; -. DR SMR; Q0TJB9; 1-362. DR GeneID; 4187436; -. DR GenomeReviews; CP000247_GR; ECP_0947. DR KEGG; ecp:ECP_0947; -. DR NMPDR; fig|340197.3.peg.2242; -. DR HOGENOM; Q0TJB9; -. DR OMA; Q0TJB9; NIFWFLP. DR BioCyc; ECOL362663:ECP_0947-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_1000066822. SQ SEQUENCE 381 AA; 41657 MW; 09146AD3B41BE936 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 NDFIPRNVAQ S //