ID   SSUD_YERPA              Reviewed;         382 AA.
AC   Q1C1S2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-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}; OrderedLocusNames=YPA_3638;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG15600.1; -; Genomic_DNA.
DR   RefSeq; WP_002210034.1; NZ_CP009906.1.
DR   AlphaFoldDB; Q1C1S2; -.
DR   SMR; Q1C1S2; -.
DR   EnsemblBacteria; ABG15600; ABG15600; YPA_3638.
DR   GeneID; 57975051; -.
DR   KEGG; ypa:YPA_3638; -.
DR   OMA; NIFWFLP; -.
DR   Proteomes; UP000001971; 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_1000066838"
SQ   SEQUENCE   382 AA;  41547 MW;  1C6798E66F573BB0 CRC64;
     MSINVFWFLP THGDGHYLGS SEGARAVDYS YLQQIAQAAD RLGFGGVLIP TGRSCEDSWL
     VAASLIPVTQ RLKFLVALRP GIISPTLAAR QAATLDRLSN GRALFNLVTG GDPEELAAEG
     LHLNHTERYE ASAEFTHVWR KVLEGETVDF AGKHIQVKGA KLLFPPVQHP RPPLYFGGSS
     AAAQDLAAEQ VELYLTWGEP PEQVKEKIEE VRAKAAAKGR TVRFGIRLHV IVRETTEEAW
     RAANRLIANL DDKTIADAQQ AFAGFDSVGQ QRMAALHGGK KDNLEISPNL WAGVGLVRGG
     AGTALVGDGP TVAQRIQEYA DLGIDTFVFS GYPHLEEAYR VSELLFPHLD LATTELPTQR
     PATQPQGEVV ANIYVPQKVS QS