ID   SSUD_YERPE              Reviewed;         382 AA.
AC   Q8ZB04; Q0WB28;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 129.
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=YPO3625, y0244, YP_3922;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(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; AL590842; CAL22213.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM83838.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS64067.1; -; Genomic_DNA.
DR   PIR; AB0441; AB0441.
DR   RefSeq; WP_002210034.1; NZ_WUCM01000052.1.
DR   RefSeq; YP_002348510.1; NC_003143.1.
DR   AlphaFoldDB; Q8ZB04; -.
DR   SMR; Q8ZB04; -.
DR   STRING; 214092.YPO3625; -.
DR   PaxDb; Q8ZB04; -.
DR   DNASU; 1145191; -.
DR   EnsemblBacteria; AAM83838; AAM83838; y0244.
DR   EnsemblBacteria; AAS64067; AAS64067; YP_3922.
DR   GeneID; 57975051; -.
DR   KEGG; ype:YPO3625; -.
DR   KEGG; ypk:y0244; -.
DR   KEGG; ypm:YP_3922; -.
DR   PATRIC; fig|214092.21.peg.4126; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_0_6; -.
DR   OMA; NIFWFLP; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0008726; F:alkanesulfonate monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0046306; P:alkanesulfonate catabolic process; IBA:GO_Central.
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..382
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_0000216722"
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