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   25-MAY-2022, entry version 104.
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   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   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., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   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.
CC       {ECO:0000250}.
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;
CC   -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000305}.
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DR   EMBL; BA000012; BAB51186.1; -; Genomic_DNA.
DR   RefSeq; WP_010912528.1; NC_002678.2.
DR   AlphaFoldDB; Q98DT4; -.
DR   SMR; Q98DT4; -.
DR   STRING; 266835.14024583; -.
DR   EnsemblBacteria; BAB51186; BAB51186; BAB51186.
DR   KEGG; mlo:mll4558; -.
DR   PATRIC; fig|266835.9.peg.3600; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_0_5; -.
DR   OMA; FIVRETD; -.
DR   Proteomes; UP000000552; 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..385
FT                   /note="Alkanesulfonate monooxygenase 2"
FT                   /id="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