ID   SSUD_YERPS              Reviewed;         382 AA.
AC   Q665B4;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=YPTB3604;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01229}.
CC   -!- MISCELLANEOUS: FMNH(2) which is absolutely required for this enzymatic
CC       reaction, is provided by SsuE. {ECO:0000255|HAMAP-Rule:MF_01229}.
CC   -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01229}.
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DR   EMBL; BX936398; CAH22842.1; -; Genomic_DNA.
DR   RefSeq; WP_011193183.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q665B4; -.
DR   SMR; Q665B4; -.
DR   EnsemblBacteria; CAH22842; CAH22842; YPTB3604.
DR   GeneID; 66843978; -.
DR   KEGG; ypo:BZ17_2996; -.
DR   KEGG; yps:YPTB3604; -.
DR   PATRIC; fig|273123.14.peg.3134; -.
DR   OMA; NIFWFLP; -.
DR   Proteomes; UP000001011; 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.
FT   CHAIN           1..382
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_0000216723"
SQ   SEQUENCE   382 AA;  41650 MW;  BBA15A227A533701 CRC64;
     MSINVFWFLP THGDGHYLGS SEGARAVDYS YLQQIAQAAD RLGFGGVLIP TGRSCEDSWL
     VAASLIPVTQ RLKFLVALRP GIISPTLAAR QAATLDRLSN GRALFNLVTG GDPEELAAEG
     LHLNHTERYE ASAEFTHVWR KVLEGETVDF AGKHIQVKGA KLLFPPVQHP RPPLYFGGSS
     AAAQDLAAEQ VELYLTWGET PEQVKEKIEE VRAKAAAKGR TVRFGIRLHV IVRETTEEAW
     RAANRLIANL DDKTIADAQQ AFARFDSVGQ QRMAALHGGK KDNLEISPNL WAGVGLVRGG
     AGTALVGDGP TVAQRIQEYA DLGIDTFVFS GYPHLEEAYR VSELLFPHLD LATTELPTQR
     PATQPQGEVV ANIYVPQKVS QS