SSUD_ERWT9
ID SSUD_ERWT9 Reviewed; 381 AA.
AC B2VC88;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=ETA_21190;
OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS 4357 / Et1/99).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=465817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA Geider K.;
RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT bacterium in the genus Erwinia.";
RL Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO97165.1; -; Genomic_DNA.
DR RefSeq; WP_012441836.1; NC_010694.1.
DR AlphaFoldDB; B2VC88; -.
DR SMR; B2VC88; -.
DR STRING; 465817.ETA_21190; -.
DR EnsemblBacteria; CAO97165; CAO97165; ETA_21190.
DR KEGG; eta:ETA_21190; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_1_0_6; -.
DR OMA; NIFWFLP; -.
DR OrthoDB; 919913at2; -.
DR Proteomes; UP000001726; 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; Reference proteome.
FT CHAIN 1..381
FT /note="Alkanesulfonate monooxygenase"
FT /id="PRO_1000139624"
SQ SEQUENCE 381 AA; 41753 MW; CB69254BADEAD06F CRC64;
MSLSVFWFLP THGDGQYLGT NEGARPVDHA YLQQIAQAAD RLGFGGVLIP TGRSCEDAWL
VAASLIPVTQ RLRFLVALRP GVISPTQAAR QAATLDRLSN GRALFNLVTG GDAEELAGDG
VFLDHRERYA ESAEFTRVWR RVLEGETVDY EGKHVHVRGA RLLFKPVQQP RPPLWFGGSS
EVAQDLAAEQ VDVYLTWGEP PAQVKEKIER VQAKAAAQGR KVRFGIRLHV IVRETNEEAW
QAADRLISHL DDETIAKAQE ALARTDSVGQ QRMAALHGGK RDRLEISPNL WAGVGLVRGG
AGTALVGDGP TVAARMQEYA DLGIETFILS GYPHLEEAYR VGELLFPHLD LVVPEIPRPA
AILAQGEHIA HQFVPQKVSQ S