ID   SSUD_PARP8              Reviewed;         385 AA.
AC   B2JKA8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=Bphy_1649;
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC70831.1; -; Genomic_DNA.
DR   RefSeq; WP_012401041.1; NZ_CADFGH010000004.1.
DR   AlphaFoldDB; B2JKA8; -.
DR   SMR; B2JKA8; -.
DR   STRING; 391038.Bphy_1649; -.
DR   EnsemblBacteria; ACC70831; ACC70831; Bphy_1649.
DR   KEGG; bph:Bphy_1649; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_0_4; -.
DR   OMA; NIFWFLP; -.
DR   OrthoDB; 919913at2; -.
DR   Proteomes; UP000001192; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..385
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_1000139612"
SQ   SEQUENCE   385 AA;  41941 MW;  7D858F25085E807F CRC64;
     MNVFWFIPTH GDSRYLGTSQ GARAADYDYF RQIAVAADTL GYEGVLLPTG RSCEDAWVVA
     SSLIPATQRL KFLVAIRPGI ASPGLSARMA ATFDRLSGGR LLINVVTGGD AAELEGDGLF
     VDHDTRYEIT DEFLRIWRGL LTSAHHGESV EFIGRHLKSK GGKLLYPPVQ SPHPPLWFGG
     SSPAAHEMAG EHIDTYLTWG EPPEAVAEKI ADIRARAAQH GRTIRFGIRL HVIVRETEDE
     AWAAADKLIS KLDDDTVARA QEAFAKMDSE GQRRMAALHG GKRGSRKELE IYPNLWAGVG
     LVRGGAGTAL VGNAEQVAAR MREYAELGIE TFILSGYPHL EESYRFAELV FPLLPGRQRA
     NANGPLSGPF GEIVGNHYAP KASQS