ID SSUD2_RHILO Reviewed; 385 AA. AC Q98DT4; DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 16-JUN-2009, entry version 36. DE RecName: Full=Alkanesulfonate monooxygenase 2; DE EC=1.14.14.5; DE AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase 2; GN Name=ssuD2; OrderedLocusNames=mll4558; OS Rhizobium loti (Mesorhizobium loti). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=381; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAFF303099; RX MEDLINE=21082930; PubMed=11214968; DOI=10.1093/dnares/7.6.331; RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., RA Takeuchi C., Yamada M., Tabata S.; RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium RT Mesorhizobium loti."; RL DNA Res. 7:331-338(2000). 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 -!- 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; BA000012; BAB51186.1; -; Genomic_DNA. DR RefSeq; NP_105400.1; -. DR HSSP; P80645; 1M41. DR GeneID; 1228061; -. DR GenomeReviews; BA000012_GR; mll4558. DR KEGG; mlo:mll4558; -. DR NMPDR; fig|266835.1.peg.3504; -. DR HOGENOM; Q98DT4; -. DR OMA; Q98DT4; HFIVRET. DR BRENDA; 1.14.14.5; 3315. 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 1 385 Alkanesulfonate monooxygenase 2. FT /FTId=PRO_0000216718. SQ SEQUENCE 385 AA; 42486 MW; A452FE24DB93FBE8 CRC64; MTSPPSPLDF FWFIPTHGDG SYLGSEEQQR PPEFGYFKQI AQAVDRLGFP GVLLPTGQNC EDSWITATGL ATLTEKLKFL VALRPGVTLP TFAARQTAAL DRLSNGRLLL NVVVGGNPTE LAGDGVFLPH DERYAQAHEF LTIWRGLVSG ERVNFDGKYY RVENGRLDLL PSQERPPLYF GGSSDAGQDL AADLVDMYLT WGEPPALVAE KLASARKKAA LRGRKLRFGI RLHFIVRETE DEAWRAADRL ISHVTDAQIE NAQARFLNQM DSVGQRRMAE LHGGRRDRLV VSPNLWAGVG LVRGGAGTAL VGTPEQVTER IREYQAIGID TIIGSGYPHL EEAYRVAELL FPRLGLGTRR QQAHRDIANE FSVGFHGAAR LQASS //