ID   SSUD1_RHILO             Reviewed;         390 AA.
AC   Q98CB9;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Alkanesulfonate monooxygenase 1;
DE            EC=1.14.14.5;
DE   AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase 1;
GN   Name=ssuD1; OrderedLocusNames=mlr5216;
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; BAB51702.1; -; Genomic_DNA.
DR   RefSeq; WP_010913041.1; NC_002678.2.
DR   AlphaFoldDB; Q98CB9; -.
DR   SMR; Q98CB9; -.
DR   STRING; 266835.14025101; -.
DR   EnsemblBacteria; BAB51702; BAB51702; BAB51702.
DR   KEGG; mlo:mlr5216; -.
DR   PATRIC; fig|266835.9.peg.4129; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_0_5; -.
DR   OMA; YGFWLPI; -.
DR   OrthoDB; 919913at2; -.
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..390
FT                   /note="Alkanesulfonate monooxygenase 1"
FT                   /id="PRO_0000216717"
FT   REGION          364..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  42332 MW;  1A5AE9184F9D6E17 CRC64;
     MTGDVPDRIK VLWFLPTHGD SRYLGTAEGG RSVDLPYLTQ VAKAADTLGY YGVLLPTGRS
     CEDSWVIASA LVPLTERLRF LVAVRPGLQS PTLAARMTAT LDRISNGRLL INVVTGGDPL
     ENKGDGIFLS HAERYEVTQE FLRIYKRVLS GETVEHQGKH LHIEDGRLLF PPVQTPYPPL
     YFGGSSDAGS TVAAQEIDKY LTWGEPPADV ERKLDAVREL AEKAGRKLSF GIRLHVIARE
     TTEEAWAAAD RLISRLDDAT IASAQKVFAR MDSVGQARMS ALHGGDRAKL EIAPNLWAGV
     GLVRGGAGTA LVGDPDTIAE RIDEYRRLGI DTFILSGYPH LEEAYRFGEL VLPKLPTDHP
     VKATGSSVNT GPFGETIAGD HRPKSLASAS