SSUD_ECO7I
ID SSUD_ECO7I Reviewed; 381 AA.
AC B7NM39;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=ECIAI39_2212;
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928164; CAR18339.1; -; Genomic_DNA.
DR RefSeq; WP_000056008.1; NC_011750.1.
DR RefSeq; YP_002408175.1; NC_011750.1.
DR AlphaFoldDB; B7NM39; -.
DR SMR; B7NM39; -.
DR STRING; 585057.ECIAI39_2212; -.
DR EnsemblBacteria; CAR18339; CAR18339; ECIAI39_2212.
DR KEGG; ect:ECIAI39_2212; -.
DR PATRIC; fig|585057.6.peg.2303; -.
DR HOGENOM; CLU_027853_1_0_6; -.
DR OMA; NIFWFLP; -.
DR Proteomes; UP000000749; 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..381
FT /note="Alkanesulfonate monooxygenase"
FT /id="PRO_1000139618"
SQ SEQUENCE 381 AA; 41716 MW; 032FF2199DC0D613 CRC64;
MSLNMFWFLP THGDGHYLGT EEGSRPVDHG YLQQIAQAAD RLGYTGVLIP TGRSCEDAWL
VEASMIPVTQ RLKFLVALRP SVTSPTVAAR QAATLDRLSN GRALFNLVTG SDPQELAGDG
VFLDHSERYE ASAEFTQVWR RLLLGETVDF NGKHIHVRGA KLLFPPIQQP YPPLYFGGSS
DVAQELAAEQ VDLYLTWGEP PELVKEKIEQ VRAKAAAHGR KIRFGIRLHV IVRETNDEAW
QAAERLISHL DDETIAKAQA AFARTDSVGQ QRMAALHNGK RDNLEISPNL WAGVGLVRGG
AGTALVGDGP TVAARINEYA ALGIDSFVLS GYPHLEEAYR VGELLFPHLD VAIPEIPQPQ
PLNPQGEAVA NDFIPRNVAQ S