ID   SSUD_PSEAE              Reviewed;         382 AA.
AC   Q9HYG2;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Alkanesulfonate monooxygenase;
DE            EC=1.14.14.5;
DE   AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase;
DE   AltName: Full=PA13;
GN   Name=ssuD; OrderedLocusNames=PA3444;
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 [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).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-14.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=9611812; DOI=10.1099/00221287-144-5-1375;
RA   Hummerjohann J., Kuttel E., Quadroni M., Ragaller J., Leisinger T.,
RA   Kertesz M.A.;
RT   "Regulation of the sulfate starvation response in Pseudomonas aeruginosa:
RT   role of cysteine biosynthetic intermediates.";
RL   Microbiology 144:1375-1386(1998).
CC   -!- FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates.
CC       {ECO:0000250}.
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 SsuE. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000305}.
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DR   EMBL; AE004091; AAG06832.1; -; Genomic_DNA.
DR   PIR; A83215; A83215.
DR   RefSeq; NP_252134.1; NC_002516.2.
DR   RefSeq; WP_003091910.1; NZ_QZGE01000037.1.
DR   AlphaFoldDB; Q9HYG2; -.
DR   SMR; Q9HYG2; -.
DR   STRING; 287.DR97_4477; -.
DR   PaxDb; Q9HYG2; -.
DR   DNASU; 879163; -.
DR   EnsemblBacteria; AAG06832; AAG06832; PA3444.
DR   GeneID; 879163; -.
DR   KEGG; pae:PA3444; -.
DR   PATRIC; fig|208964.12.peg.3606; -.
DR   PseudoCAP; PA3444; -.
DR   HOGENOM; CLU_027853_1_0_6; -.
DR   InParanoid; Q9HYG2; -.
DR   OMA; NIFWFLP; -.
DR   PhylomeDB; Q9HYG2; -.
DR   BioCyc; PAER208964:G1FZ6-3512-MON; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Flavoprotein; FMN; Monooxygenase;
KW   Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9611812"
FT   CHAIN           2..382
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_0000216711"
FT   CONFLICT        7
FT                   /note="W -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   382 AA;  41567 MW;  BF2C6EE4A1E102CD CRC64;
     MSLEIFWFLP THGDGHYLGT TQGARAVDHG YLQQIAQAAD RLGFGGVLIP TGRSCEDSWL
     VAASLIPVTQ RLKFLVALRP GIISPTVAAR QAATLDRLSN GRALFNLVTG GDPDELAGDG
     LHLSHAERYE ASVEFTRIWR RVLEGETVDY AGKHIQVKGA KLLYPPLQQP RPPLYFGGSS
     EAAQDLAAEQ VELYLTWGEP PAAVAEKIAQ VREKAARQGR QVRFGIRLHV IVRETSEEAW
     QAADRLIAHL DDDTIARAQA SLARFDSVGQ QRMAALHGGS RDNLEVSPNL WAGVGLVRGG
     AGTALVGDGP TVAARVREYA ELGIDTFIFS GYPHLEESYR VAELLFPHLD VQRPAQPEGR
     GYVSPFGEMV ANDILPRQAA QS