ID SSUD_ENT38 Reviewed; 381 AA. AC A4W8V4; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 16-JUN-2009, entry version 14. DE RecName: Full=Alkanesulfonate monooxygenase; DE EC=1.14.14.5; DE AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase; GN Name=ssuD; OrderedLocusNames=Ent638_1454; OS Enterobacter sp. (strain 638). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=399742; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., RA Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L., RA Vangronsveld J., van der Lelie D., Richardson P.; RT "Complete sequence of chromosome of Enterobacter sp. 638."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000653; ABP60134.1; -; Genomic_DNA. DR RefSeq; YP_001176185.1; -. DR GeneID; 5114419; -. DR GenomeReviews; CP000653_GR; Ent638_1454. DR KEGG; ent:Ent638_1454; -. DR NMPDR; fig|399742.4.peg.1445; -. DR OMA; A4W8V4; NIFWFLP. 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_1000066824. SQ SEQUENCE 381 AA; 41795 MW; B4691862C7A81F9B CRC64; MSLNLFWFLP THGDGHYLGT EEGARPVDYG YLQQIAQAAD RIGFTGVLIP TGRSCEDAWL VAAAMIPVTQ RLKFLVALRP SVVSPTVAAR QAATLDRLSN GRALFNLVTG SDPTELAGDG VFLDHTERYE ASAEFTRVWR RLLEGDTVTY EGKHIRVRDA KLYFPPVQQP RPPLYFGGSS DVAQDLAAEQ VDLYLTWGEP PEQVKEKIEQ VRAKAAAHGR KVRFGIRLHV IVRETNQEAW QAADRLISHL DDDTIAKAQA ALAKTDSVGQ HRMASLHNGK RENLEISPNL WAGVGLVRGG AGTALVGDGP TVAARINEYA DLGIDSFILS GYPHLEEAYN VGELLFPHLD VAIPEIPQPR PLQVQGEAVA NEFIPRKTAQ S //