ID   SSUD_BURTA              Reviewed;         384 AA.
AC   Q2SVM8;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   25-MAY-2022, entry version 91.
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=BTH_I2501;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABC38862.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000086; ABC38862.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_009891371.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2SVM8; -.
DR   SMR; Q2SVM8; -.
DR   EnsemblBacteria; ABC38862; ABC38862; BTH_I2501.
DR   KEGG; bte:BTH_I2501; -.
DR   HOGENOM; CLU_027853_1_0_4; -.
DR   OrthoDB; 919913at2; -.
DR   Proteomes; UP000001930; Chromosome I.
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..384
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_0000403214"
SQ   SEQUENCE   384 AA;  41856 MW;  65328CA7F117D0FD CRC64;
     MNVFWFIPTH GDSRYLGTAE GARAADYDYF RQVAVAADTL GYDGVLLPTG RSCEDAWVVA
     SSLIPATKRL KFLVAIRPGL SSPGLSARMA STFDRLSGGR LLINVVTGGD SAELEGDGLF
     ADHDTRYALT DDFLHIWRKL LAESHENGSV DFDGEHLRAK GGKLLYPPIQ HPHPPLWFGG
     SSPAAHAIAA DHIETYLTWG EPPAAVAKKI ADIRARAAER GREIRFGIRL HVIVRETEEE
     AWRDADRLIS RLDDDTIARA QQAFAKMDSE GQRRMAALHG GKRGSRQELE IYPNLWAGVG
     LVRGGAGTAL VGNPEQVAAR MREYAALGIE TFILSGYPHL EESYRFAELV FPLVKGGDAR
     RAGPLSGPFG EVVGNGYLPK VSQS