ID   SSUD_CUPPJ              Reviewed;         387 AA.
AC   Q46ZU3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Alkanesulfonate monooxygenase {ECO:0000255|HAMAP-Rule:MF_01229};
DE            EC=1.14.14.5 {ECO:0000255|HAMAP-Rule:MF_01229};
DE   AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase {ECO:0000255|HAMAP-Rule:MF_01229};
GN   Name=ssuD {ECO:0000255|HAMAP-Rule:MF_01229}; OrderedLocusNames=Reut_A1976;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
CC   -!- FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates.
CC       {ECO:0000255|HAMAP-Rule:MF_01229}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + 2 H(+) +
CC         H2O + sulfite; Xref=Rhea:RHEA:23064, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17359,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:134249; EC=1.14.14.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01229};
CC   -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01229}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000090; AAZ61340.1; -; Genomic_DNA.
DR   RefSeq; WP_011298138.1; NC_007347.1.
DR   AlphaFoldDB; Q46ZU3; -.
DR   SMR; Q46ZU3; -.
DR   STRING; 264198.Reut_A1976; -.
DR   EnsemblBacteria; AAZ61340; AAZ61340; Reut_A1976.
DR   KEGG; reu:Reut_A1976; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_0_4; -.
DR   OMA; NIFWFLP; -.
DR   OrthoDB; 919913at2; -.
DR   GO; GO:0008726; F:alkanesulfonate monooxygenase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.30; -; 1.
DR   HAMAP; MF_01229; Alkanesulf_monooxygen; 1.
DR   InterPro; IPR019911; Alkanesulphonate_mOase_FMN-dep.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   SUPFAM; SSF51679; SSF51679; 1.
DR   TIGRFAMs; TIGR03565; alk_sulf_monoox; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..387
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_1000066833"
SQ   SEQUENCE   387 AA;  41832 MW;  156CD1112733D5C5 CRC64;
     MQVFWFIPTH GDSRYLGTSE GAREVGIDYL KQVAVAADTL GYEGVLIPTG RSCEDPWVVA
     SALAAVTQKL RFLVAVRPGL MTPTLAARMA ATFDRISGGR LLVNLVTGGD VAELEGDGLF
     LDHAARYEAS SEFIRIWRDV LAASHDSGEI SFKGRHLRVK GARVLYPPLQ RPHPPVYFGG
     SSAAAHELAG EQVDTYLTWG EPPADVALKL ADVRKHAERH GRTVKFGIRL HVIVRETEAA
     AWAAADDLIS RLDDETVARA QAVFAKMDSE GQRRMAALHA GGSKRTREAL EISPNLWAGV
     GLVRGGAGTA LVGDPHQVAA RIREYSELGI DTFVLSGYPH LEEAYRFAEL VFPLLPLAVR
     NKLPGQVLSG PFGEVMATGI VPRASQS