ID   SSUD_BURP1              Reviewed;         385 AA.
AC   Q3JSR8;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   03-AUG-2022, entry version 88.
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};
GN   OrderedLocusNames=BURPS1710b_1989;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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=ABA49294.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000124; ABA49294.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004192866.1; NC_007434.1.
DR   AlphaFoldDB; Q3JSR8; -.
DR   SMR; Q3JSR8; -.
DR   EnsemblBacteria; ABA49294; ABA49294; BURPS1710b_1989.
DR   GeneID; 56595649; -.
DR   KEGG; bpm:BURPS1710b_1989; -.
DR   HOGENOM; CLU_027853_1_0_4; -.
DR   OrthoDB; 919913at2; -.
DR   Proteomes; UP000002700; 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..385
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_0000403213"
SQ   SEQUENCE   385 AA;  41849 MW;  46902CEBEB65BE84 CRC64;
     MNVFWFIPTH GDSRYLGTAE GARAADYDYF RQVAVAADTL GYDGVLLPTG RSCEDAWVVA
     SSLIPATKRL KFLVAIRPGL SSPGLSARMA STFDRLSDGR LLINVVTGGD SAELEGDGLF
     ADHDTRYAIT DDFLHIWRGL LAESHENGGI DFDGEHLSAK GGKLLYPPVQ RPHPPLWFGG
     SSPAAHAIAA DHIDTYLSWG EPPAAVEKKI ADIRARAAAR GREIKFGIRL HVIVRETQEE
     AWRDADRLIS RLDDDTIARA QQAFAKMDSE GQRRMAALHG GKRGSRQELE IYPNLWAGVG
     LVRGGAGTAL VGNPEQIAAR MREYAALGIE TFILSGYPHL EESYRFAELV FPLVKGGGNT
     RRAGPLSGPF GEVVGNQYLP KASQS