SSUD_PSEMY
ID SSUD_PSEMY Reviewed; 382 AA.
AC A4Y0F3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Pmen_4322;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000255|HAMAP-
CC Rule:MF_01229}.
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DR EMBL; CP000680; ABP87069.1; -; Genomic_DNA.
DR RefSeq; WP_012020096.1; NC_009439.1.
DR AlphaFoldDB; A4Y0F3; -.
DR SMR; A4Y0F3; -.
DR STRING; 399739.Pmen_4322; -.
DR EnsemblBacteria; ABP87069; ABP87069; Pmen_4322.
DR KEGG; pmy:Pmen_4322; -.
DR PATRIC; fig|399739.8.peg.4374; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_1_0_6; -.
DR OMA; NIFWFLP; -.
DR OrthoDB; 919913at2; -.
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_1000066829"
SQ SEQUENCE 382 AA; 41308 MW; AFCB414A88E87DEF CRC64;
MSLNIFWFLP THGDGKYLGT AEGARAVDHG YLAQIAQAAD RLGYGGVLIP TGRSCEDSWL
VAASLIPVTQ NLKFLVALRP GIISPTVAAR QAATLDRLSN ARALFNLVTG GDPDELAGDG
LHLSHAERYE ASVEFTRIWR RVLEGETVDY DGKHIQVKGA KLLYPPIQQP RPPLYFGGSS
DAAQDLAAEQ VELYLTWGEP PAAVAEKIAQ VREKAARQGR EVRFGIRLHV IVRETNEEAW
AAADRLISHL DQDTIDRAQA SLARFDSVGQ QRMAALHGGK TDNLEVSPNL WAGVGLVRGG
AGTALVGDGP TVAARVREYA ELGIDTFIFS GYPHLEESYR VAELLFPHLD VAPPARPESR
GYVSPFGEMI SSDILPKAAA AS