SSUD_CROS8
ID SSUD_CROS8 Reviewed; 381 AA.
AC A7MEW3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-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=ESA_02405;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU77651.1; -; Genomic_DNA.
DR RefSeq; WP_012125195.1; NC_009778.1.
DR AlphaFoldDB; A7MEW3; -.
DR SMR; A7MEW3; -.
DR EnsemblBacteria; ABU77651; ABU77651; ESA_02405.
DR KEGG; esa:ESA_02405; -.
DR PATRIC; fig|290339.8.peg.2137; -.
DR HOGENOM; CLU_027853_1_0_6; -.
DR OMA; NIFWFLP; -.
DR OrthoDB; 919913at2; -.
DR Proteomes; UP000000260; 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_1000066825"
SQ SEQUENCE 381 AA; 41482 MW; 90C55795D71BC381 CRC64;
MSLNLFWFLP THGDGHYLGS DAGARPVDHG YLQQIAQAAD RLGFTGVLIP TGRSCEDAWL
VAASMIPVTQ RLKFLVALRP SVVSPTVAAR QAATLDRLSN GRALFNLVTG SDPQELAGDG
VFLDHTARYE ASAEFTRVWR RLLEGEKVDF EGKHIKVRGA QLLFPPVQQP RPPLYFGGSS
DVAQDLAAEQ VDLYLTWGEP PEQVKEKIAQ VRAKAAAHGR TVRFGIRLHV IVRETTEEAW
QAADRLIAHL DDETIAKAQA AFARQDSVGQ QRMAALHGGR RDQLEISPNL WAGVGLVRGG
AGTALVGDGP TVAARINEYA ALGIDSFILS GYPHLEEAYR VGEFLFPHLD VAIPDVPQPR
PLTAQGEAVA NEFIPRRVAQ S