ID SSUD_XANAC Reviewed; 387 AA. AC Q8PP38; DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 35. DE RecName: Full=Alkanesulfonate monooxygenase; DE EC=1.14.14.5; DE AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase; GN Name=ssuD; OrderedLocusNames=XAC0850; OS Xanthomonas axonopodis pv. citri (Citrus canker). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=92829; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., RA Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing RT host specificities."; RL Nature 417:459-463(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 -!- 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; AE011716; AAM35738.1; -; Genomic_DNA. DR RefSeq; NP_641202.1; -. DR HSSP; P80645; 1M41. DR SMR; Q8PP38; 1-355. DR GeneID; 1154921; -. DR GenomeReviews; AE008923_GR; XAC0850. DR KEGG; xac:XAC0850; -. DR NMPDR; fig|190486.1.peg.846; -. DR HOGENOM; Q8PP38; -. DR OMA; Q8PP38; NIFWFLP. DR BioCyc; XAXO190486:XAC0850-MON; -. DR BRENDA; 1.14.14.5; 289771. 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 Gene3D; G3DSA:3.20.20.30; Luciferase_like; 1. DR TIGRFAMs; TIGR03565; Alk_sulf_monoox; 1. PE 3: Inferred from homology; KW Complete proteome; FMN; Monooxygenase; Oxidoreductase. FT CHAIN 1 387 Alkanesulfonate monooxygenase. FT /FTId=PRO_0000216721. SQ SEQUENCE 387 AA; 42084 MW; 14DD75B0AE505620 CRC64; MDMFWFIPTH GDSRYLGTSD GARQVSAEYV TQVAVAADTL GYEGVLIPTG RSCEDPWVIA SSLINATRRL KFLVALRPGL MAPALAARTA ASFDRLSGGR LLVNLVTGGD RGELEGDGVF LDHAERYEAS AEFIRIWREI IAHSHSGESY DFDGKHLQVK AAKLLYPTVQ RPYPPVWFGG SSDAAHDLAA EQVDTYLTWG EPPDAVAEKI ASVRSKAAAL GRTLTFGIRL HVIVRETEAE AWAAAESLIS HLDDETVERA QSAFARMDSV GQRRMAALHS RGQRRTRADL EVSPNLWAGV GLVRGGAGTA LVGDPQTVAK RIEEYAALGI DTFIFSGYPH LEEAYRFAEL VFPLLPRTVK QKLPGQALSG PFGEVIANTI VPRASAR //