SSUD_YERPB
ID SSUD_YERPB Reviewed; 382 AA.
AC B2K4U5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=YPTS_3794;
OS Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1/+;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL Submitted (APR-2008) 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 -!- 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; CP001048; ACC90747.1; -; Genomic_DNA.
DR RefSeq; WP_011193183.1; NZ_CP009780.1.
DR AlphaFoldDB; B2K4U5; -.
DR SMR; B2K4U5; -.
DR GeneID; 66843978; -.
DR KEGG; ypb:YPTS_3794; -.
DR PATRIC; fig|502801.10.peg.3259; -.
DR OMA; NIFWFLP; -.
DR BioCyc; YPSE502801:YPTS_RS19125-MON; -.
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_1000139629"
SQ SEQUENCE 382 AA; 41650 MW; BBA15A227A533701 CRC64;
MSINVFWFLP THGDGHYLGS SEGARAVDYS YLQQIAQAAD RLGFGGVLIP TGRSCEDSWL
VAASLIPVTQ RLKFLVALRP GIISPTLAAR QAATLDRLSN GRALFNLVTG GDPEELAAEG
LHLNHTERYE ASAEFTHVWR KVLEGETVDF AGKHIQVKGA KLLFPPVQHP RPPLYFGGSS
AAAQDLAAEQ VELYLTWGET PEQVKEKIEE VRAKAAAKGR TVRFGIRLHV IVRETTEEAW
RAANRLIANL DDKTIADAQQ AFARFDSVGQ QRMAALHGGK KDNLEISPNL WAGVGLVRGG
AGTALVGDGP TVAQRIQEYA DLGIDTFVFS GYPHLEEAYR VSELLFPHLD LATTELPTQR
PATQPQGEVV ANIYVPQKVS QS