ID   SSUD_PSESM              Reviewed;         379 AA.
AC   Q87ZG3;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=PSPTO_3466;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO56941.1; -; Genomic_DNA.
DR   RefSeq; NP_793246.1; NC_004578.1.
DR   RefSeq; WP_011104574.1; NC_004578.1.
DR   AlphaFoldDB; Q87ZG3; -.
DR   SMR; Q87ZG3; -.
DR   STRING; 223283.PSPTO_3466; -.
DR   EnsemblBacteria; AAO56941; AAO56941; PSPTO_3466.
DR   GeneID; 1185131; -.
DR   KEGG; pst:PSPTO_3466; -.
DR   PATRIC; fig|223283.9.peg.3548; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_0_6; -.
DR   OMA; YGFWLPI; -.
DR   OrthoDB; 919913at2; -.
DR   PhylomeDB; Q87ZG3; -.
DR   Proteomes; UP000002515; 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; Reference proteome.
FT   CHAIN           1..379
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_0000216714"
SQ   SEQUENCE   379 AA;  41604 MW;  10AD306482C0A6C9 CRC64;
     MNVFWFLPTH GDGHYLGTTK GARPVTLNYL KQVAQAADDL GYYGVLIPTG RSCEDSWVIA
     SALVPLTERL KYLVAIRPGI ISPTVSARMA ATLDRLSGGR LLINVVTGGD PDENRGDGSF
     LDHSERYEVT DEFLHIWRRV LQGEAVDFEG KHLRVQNAKA LYPPIQKPYP PLYFGGSSDA
     AHDLAADQVD VYLTWGEPPA AVAQKLADVR ERAARKGRTV KFGIRLHVIV RQTSEEAWKA
     ASTLIEHISD ETIAAAQKSF SRFDSEGQRR MAALHDGRRD NLEIAPNLWA GVGLVRGGAG
     TALVGNPQEV AERIKEYADL GIESFIFSAY PHLEEAYRFA ELVFPLLPEP YASLAGRGIT
     NLTGPFGEMI ANDLPPQAK