ID D2TS72_CITRI Unreviewed; 381 AA.
AC D2TS72;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Alkanesulfonate monooxygenase {ECO:0000256|ARBA:ARBA00012113, ECO:0000256|HAMAP-Rule:MF_01229};
DE EC=1.14.14.5 {ECO:0000256|ARBA:ARBA00012113, ECO:0000256|HAMAP-Rule:MF_01229};
DE AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase {ECO:0000256|HAMAP-Rule:MF_01229};
GN Name=ssuD1 {ECO:0000313|EMBL:CBG87783.1};
GN Synonyms=ssuD {ECO:0000256|HAMAP-Rule:MF_01229};
GN OrderedLocusNames=ROD_10041 {ECO:0000313|EMBL:CBG87783.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG87783.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG87783.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG87783.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
CC -!- FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates.
CC {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01229};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01229}.
CC -!- MISCELLANEOUS: FMNH(2) which is absolutely required for this enzymatic
CC reaction, is provided by SsuE. {ECO:0000256|HAMAP-Rule:MF_01229}.
CC -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000256|ARBA:ARBA00007044,
CC ECO:0000256|HAMAP-Rule:MF_01229}.
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DR EMBL; FN543502; CBG87783.1; -; Genomic_DNA.
DR RefSeq; WP_012905327.1; NC_013716.1.
DR AlphaFoldDB; D2TS72; -.
DR STRING; 637910.ROD_10041; -.
DR KEGG; cro:ROD_10041; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_1_0_6; -.
DR OrthoDB; 9814695at2; -.
DR Proteomes; UP000001889; Chromosome.
DR GO; GO:0008726; F:alkanesulfonate monooxygenase activity; IEA:UniProtKB-UniRule.
DR CDD; cd01094; Alkanesulfonate_monoxygenase; 1.
DR Gene3D; 3.20.20.30; Luciferase-like domain; 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 NCBIfam; TIGR03565; alk_sulf_monoox; 1.
DR PANTHER; PTHR42847; ALKANESULFONATE MONOOXYGENASE; 1.
DR PANTHER; PTHR42847:SF4; ALKANESULFONATE MONOOXYGENASE-RELATED; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01229};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01229};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_01229};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01229}.
FT DOMAIN 5..325
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
SQ SEQUENCE 381 AA; 41706 MW; 0FEF26DEE98A2E24 CRC64;
MSLNMFWFLP THGDGHYLGT DEGARPVDHS YLQQIAQTAD RLGFTGVLIP TGRSCEDAWL
VAASMIPVTR RLKFLVALRP SVTSPTVAAR QAATLDRLSD GRALFNLVTG SDPQELAGDG
VFLNHTERYE ASAEFTQVWR RLLQGETVDF NGKHIHVNGA KLFFPPVQQP HPPLYFGGSS
DVAQDLAAEQ VDLYLTWGEP PEQVKEKIAQ VRAKAAARGR TIRFGIRLHV IVRETNDEAW
RAADRLIAHL DDDTIAKAQA AFARTDSVGQ QRMAALHNGR RDKLEISPNL WAGVGLVRGG
AGTALVGDGP IVAARINEYA ALGIDSFVLS GYPHLEEAWK VGELLFPHLD VATPAIPQPQ
RRHLQGEAVA NDFIPQKVAQ S
//
