ID SSUD_POLNA Reviewed; 387 AA.
AC A1VPZ7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
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=Pnap_2418;
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2;
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(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 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 -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000255|HAMAP-
CC Rule:MF_01229}.
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DR EMBL; CP000529; ABM37725.1; -; Genomic_DNA.
DR RefSeq; WP_011801803.1; NC_008781.1.
DR AlphaFoldDB; A1VPZ7; -.
DR SMR; A1VPZ7; -.
DR STRING; 365044.Pnap_2418; -.
DR KEGG; pna:Pnap_2418; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_1_0_4; -.
DR OrthoDB; 9814695at2; -.
DR Proteomes; UP000000644; 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; FMN; Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..387
FT /note="Alkanesulfonate monooxygenase"
FT /id="PRO_1000066826"
SQ SEQUENCE 387 AA; 42159 MW; BED503F658B768D0 CRC64;
MQVFWFIPTH GDSRYLGTGE GAREVSHDYL KQVAIAADTQ GYDGVLIPTG RSCEDPWVVA
SSLISATKNL KFLVAVRPGL HQPSLAARMA ATFDRLSGGR LLINLVTGGD QAELEGDGVS
LGHAERYEQS AEFIRIWREI IARSHTGESF DYEGKHLSVK GAKLLYPPVQ KPYPLVYFGG
SSPAAHDLAA EQVDAYLTWG EPPAEVAKKI ADVRARAAKF GRTVKFGIRL HVIVRETDDE
AWRAAESLIS RLDDDTVIRA QAAFSRMDSE GQRRMAALHA GGKKRTRADL EISPNLWAGV
GLVRGGAGTA LVGDAKTVAA RIEEYAALGI DTFVFSGYPH LEEAYRFAEL VFPLLPRKLR
QKLPGTGLTG PFGEVVANSY LPRVSQS
//
