ID   MSUD_PSEAE              Reviewed;         381 AA.
AC   Q9I1C2; O31039;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Methanesulfonate monooxygenase;
DE            EC=1.14.14.5;
DE   AltName: Full=FMNH2-dependent methanesulfonate monooxygenase;
DE   AltName: Full=Methanesulfonate sulfonatase;
GN   Name=msuD; OrderedLocusNames=PA2356;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10049377; DOI=10.1128/jb.181.5.1464-1473.1999;
RA   Kertesz M.A., Schmidt-Larbig K., Wueest T.;
RT   "A novel reduced flavin mononucleotide-dependent methanesulfonate
RT   sulfonatase encoded by the sulfur-regulated msu operon of Pseudomonas
RT   aeruginosa.";
RL   J. Bacteriol. 181:1464-1473(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates. Shows
CC       highest activity with methanesulfonate. {ECO:0000269|PubMed:10049377}.
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;
CC   -!- INDUCTION: Repressed by sulfate, cysteine, or thiocyanate.
CC   -!- MISCELLANEOUS: FMNH(2) which is absolutely required for this enzymatic
CC       reaction, is provided by MsuE.
CC   -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000305}.
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DR   EMBL; AF026067; AAB82564.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG05744.1; -; Genomic_DNA.
DR   PIR; E83352; E83352.
DR   RefSeq; NP_251046.1; NC_002516.2.
DR   RefSeq; WP_003104713.1; NZ_QZGE01000021.1.
DR   AlphaFoldDB; Q9I1C2; -.
DR   SMR; Q9I1C2; -.
DR   STRING; 287.DR97_6076; -.
DR   PaxDb; Q9I1C2; -.
DR   PRIDE; Q9I1C2; -.
DR   EnsemblBacteria; AAG05744; AAG05744; PA2356.
DR   GeneID; 879651; -.
DR   KEGG; pae:PA2356; -.
DR   PATRIC; fig|208964.12.peg.2465; -.
DR   PseudoCAP; PA2356; -.
DR   HOGENOM; CLU_027853_1_0_6; -.
DR   InParanoid; Q9I1C2; -.
DR   OMA; YGFWLPI; -.
DR   PhylomeDB; Q9I1C2; -.
DR   BioCyc; PAER208964:G1FZ6-2395-MON; -.
DR   BRENDA; 1.14.14.34; 5087.
DR   Proteomes; UP000002438; 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   2: Evidence at transcript level;
KW   Flavoprotein; FMN; Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..381
FT                   /note="Methanesulfonate monooxygenase"
FT                   /id="PRO_0000216710"
FT   CONFLICT        28
FT                   /note="P -> S (in Ref. 1; AAB82564)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  41596 MW;  F39FF1C2E3217747 CRC64;
     MNVFWFLPTH GDGHFLGTSQ GARPVSLPYL KQVAQAADSL GYHGVLIPTG RSCEDSWVVA
     SALAPLTERL RFLVAIRPGI VSPTVSARMA ATLDRLSGGR LLINVVTGGD PDENRGDGIH
     LGHAERYEVT DEFLRVWRRV LQGEAVDFHG KHIHVENAKA LYPPLQRPYP PLYFGGSSEA
     AHELAGEQVD VYLTWGEPLP AVAAKIADVR QRAARHGRTV KFGIRLHVIV RETAEEAWRA
     ADRLIEHISD ETIAAAQQSF ARFDSEGQRR MAALHGGRRD RLEIQPNLWA GVGLVRGGAG
     TALVGDPRQV AERIGEYAEL GIDSFIFSGY PHLEEAYRFA ELVFPLLPEP YASLAGRGLT
     NLTGPFGEMI ANDVLPARAG A