ID   SSUD_METC4              Reviewed;         391 AA.
AC   B7KX11;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Mchl_3717;
OS   Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS   extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=440085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM4 / NCIMB 13688;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT   CM4.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001298; ACK84536.1; -; Genomic_DNA.
DR   RefSeq; WP_003606053.1; NC_011757.1.
DR   AlphaFoldDB; B7KX11; -.
DR   SMR; B7KX11; -.
DR   EnsemblBacteria; ACK84536; ACK84536; Mchl_3717.
DR   KEGG; mch:Mchl_3717; -.
DR   HOGENOM; CLU_027853_1_0_5; -.
DR   OMA; NIFWFLP; -.
DR   BioCyc; MEXT440085:MCHL_RS18095-MON; -.
DR   Proteomes; UP000002385; Chromosome.
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..391
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_1000164970"
SQ   SEQUENCE   391 AA;  42591 MW;  2738350FE4E142C0 CRC64;
     MTIQTDGKTD VLWFLPTHGD GRYLGASEGA RDVSLPYLRQ IAQAADDLGY YGVLLPTGRS
     CEDSWVVASA LAPLTQRLRF LVAVRPGLQE PSMAARMAAT LDRISDGRLL INVVTGGDPV
     ELKGDGVFLD HDERYVVTDE FLHIWRGLMA GETVNFEGKH LRSENGRVIF RPVQAPYPPL
     YFGGSSPAGI EVAAEHCEVY LTWGEPPAGV AEKIAKAREA AERKGKTFSY GIRLHVIVRE
     TESEAWEAAD RLISRLDDAT IAQAQATLKR QDSVGQSRMM ALHGGDRNKL VVSPNLWAGV
     GLVRGGAGTA LVGSADQVAD RMKEYIDLGI DRFILSGYPH LEEAYRFAEL VFPKLPLRAT
     TGTAPSTARN NGPFGEVIAN DIVPTRRVSA H