(data stored in ACNUC7421 zone)

SWISSPROT: SSUD_ESCF3

ID   SSUD_ESCF3              Reviewed;         381 AA.
AC   B7LNV2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
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=EFER_1079;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / CDC 0568-73;
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.,
RA   Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA   Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA   Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA   Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA   Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA   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
CC         H(+) + 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
CC       enzymatic reaction, is provided by SsuE. {ECO:0000255|HAMAP-
CC       Rule:MF_01229}.
CC   -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01229}.
DR   EMBL; CU928158; CAQ88608.1; -; Genomic_DNA.
DR   RefSeq; WP_000056012.1; NC_011740.1.
DR   SMR; B7LNV2; -.
DR   PRIDE; B7LNV2; -.
DR   EnsemblBacteria; CAQ88608; CAQ88608; EFER_1079.
DR   KEGG; efe:EFER_1079; -.
DR   HOGENOM; HOG000134568; -.
DR   KO; K04091; -.
DR   OMA; NIFWFLP; -.
DR   OrthoDB; 919913at2; -.
DR   BioCyc; EFER585054:EFER_RS05480-MONOMER; -.
DR   Proteomes; UP000000745; 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;
DR   PRODOM; B7LNV2.
DR   SWISS-2DPAGE; B7LNV2.
KW   Complete proteome; Flavoprotein; FMN; Monooxygenase; Oxidoreductase.
FT   CHAIN         1    381       Alkanesulfonate monooxygenase.
FT                                /FTId=PRO_1000139625.
SQ   SEQUENCE   381 AA;  41643 MW;  D08F11C018B9E401 CRC64;
     MSLNMFWFLP THGDGHYLGT EEGSRSVDHG YLQQIAQVAD RLGYTGVLIP TGRSCEDAWL
     VAASMIPVTQ RLKFLVALRP SVTSPTVAAR QAATLDRLSN GRALFNLVTG SDPQELAGDG
     VFLDHSERYE ASAEFTQVWR RLLLGETVDF NGKHIHVRGA KLLFPPIQQP YPPLYFGGSS
     DVAQDLAAEQ VDLYLTWGEP PELVKEKIAH VRAKAAAHGR KIRFGIRLHV IVRETNDEAW
     QAAERLISHL DDETIAKAQA AFARTDSVGQ QRMAALHNGK RDNLEISPNL WAGVGLVRGG
     AGTALVGDGP TVAARINEYA ALGIDSFVLS GYPHLEEAYR IGELLFPHLD VAIPEIPQPQ
     LLNPQGEAVA NDFIPRNVAQ S
//

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