ID   SSUD_BRADU              Reviewed;         387 AA.
AC   Q89ER2;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=bll7010;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC52275.1; -; Genomic_DNA.
DR   RefSeq; NP_773650.1; NC_004463.1.
DR   RefSeq; WP_011089747.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89ER2; -.
DR   SMR; Q89ER2; -.
DR   STRING; 224911.27355291; -.
DR   EnsemblBacteria; BAC52275; BAC52275; BAC52275.
DR   GeneID; 64026764; -.
DR   KEGG; bja:bll7010; -.
DR   PATRIC; fig|224911.44.peg.7052; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_0_5; -.
DR   InParanoid; Q89ER2; -.
DR   OMA; NIFWFLP; -.
DR   PhylomeDB; Q89ER2; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0008726; F:alkanesulfonate monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0046306; P:alkanesulfonate catabolic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..387
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_0000216704"
FT   REGION          365..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   387 AA;  42411 MW;  C63361B094AD8431 CRC64;
     MSQSKSNILW FLPTHGDGRY LGTATGGREV NFNYLRQIAQ AADQLGYFGV LLPTGRSCED
     SWIVASSVAP FTERLRYLVA VRPGLQSPSV AARMTATLDR ITNGRLLINV VTGGDPVENK
     GDGIFLGHDE RYEVTREFLN VYSDLLGGKA VNVEGKHIRI EDGKLLFPPV QSPRPPLYFG
     GSSDAGIDVA VDTVDKYLTW GEPPAQVAEK IARVREVANA RGRKLSFGIR LHVIVRETNE
     EAWSAANELI KHVSDDTIAR AQRNFARMDS VGQQRMAQLH GGKRDKLEIS PNLWAGVGLV
     RGGAGTALVG DAQTVAARIK EYQDIGIDTF IMSGYPHLEE AYRFAELVFP LLSLDHGSNV
     TRLHHNSGPF GETVGNDYRP SRLASQS