SSUD_PSEPU
ID SSUD_PSEPU Reviewed; 382 AA.
AC O85764; Q8KZQ8; Q9KHR0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Alkanesulfonate monooxygenase;
DE EC=1.14.14.5;
DE AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase;
GN Name=ssuD; Synonyms=dsuD;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6884 / S-313;
RX PubMed=10781557; DOI=10.1128/jb.182.10.2869-2878.2000;
RA Kahnert A., Vermeij P., Wietek C., James P., Leisinger T., Kertesz M.A.;
RT "The ssu locus plays a key role in organosulfur metabolism in Pseudomonas
RT putida S-313.";
RL J. Bacteriol. 182:2869-2878(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Rot18;
RA Kertesz M.A., Sialm M.;
RT "Sulfur-controlled aryl desulfonation phenotypes in Pseudomonas spp. and
RT other soil isolates, and conservation of the sulfonate monooxygenase gene
RT (ssuD).";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DS1;
RX PubMed=12835925; DOI=10.1007/s00253-003-1233-7;
RA Endoh T., Kasuga K., Horinouchi M., Yoshida T., Habe H., Nojiri H.,
RA Omori T.;
RT "Characterization and identification of genes essential for dimethyl
RT sulfide utilization in Pseudomonas putida strain DS1.";
RL Appl. Microbiol. Biotechnol. 62:83-91(2003).
CC -!- FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates. Seems
CC also to be involved in the desulfurization of aromatic sulfonates.
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;
CC -!- INDUCTION: Repressed by sulfate, cysteine, or thiocyanate.
CC -!- MISCELLANEOUS: FMNH(2) which is absolutely required for this enzymatic
CC reaction, is provided by SsuE.
CC -!- SIMILARITY: Belongs to the SsuD family. {ECO:0000305}.
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DR EMBL; AF075709; AAC31905.1; -; Genomic_DNA.
DR EMBL; AF250870; AAF81713.1; -; Genomic_DNA.
DR EMBL; AB086390; BAC00973.1; -; Genomic_DNA.
DR AlphaFoldDB; O85764; -.
DR SMR; O85764; -.
DR STRING; 1240350.AMZE01000010_gene3811; -.
DR eggNOG; COG2141; Bacteria.
DR BioCyc; MetaCyc:MON-14252; -.
DR BRENDA; 1.14.14.34; 5092.
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 2: Evidence at transcript level;
KW Flavoprotein; FMN; Monooxygenase; Oxidoreductase.
FT CHAIN 1..382
FT /note="Alkanesulfonate monooxygenase"
FT /id="PRO_0000216713"
FT CONFLICT 21
FT /note="S -> N (in Ref. 2; AAF81713)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="E -> D (in Ref. 1; AAC31905)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="Q -> E (in Ref. 1; AAC31905)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="L -> F (in Ref. 2; AAF81713)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="V -> N (in Ref. 1; AAC31905)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="I -> V (in Ref. 1; AAC31905)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="E -> D (in Ref. 2; AAF81713)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="S -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="E -> Q (in Ref. 2; AAF81713)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="D -> E (in Ref. 2; AAF81713)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="K -> R (in Ref. 1; AAC31905)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="N -> G (in Ref. 1; AAC31905)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="N -> K (in Ref. 2; AAF81713)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="K -> N (in Ref. 1; AAC31905)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="K -> Q (in Ref. 2; AAF81713)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="E -> D (in Ref. 1; AAC31905)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="L -> I (in Ref. 1; AAC31905)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="Q -> I (in Ref. 2; AAF81713)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="A -> P (in Ref. 1; AAC31905)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="T -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="S -> G (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 370..371
FT /note="VA -> C (in Ref. 2; AAF81713)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="A -> S (in Ref. 1; AAC31905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 41553 MW; B9117539DFF5DDAD CRC64;
MSLNIFWFLP THGDGKYLGT SEGARAVDHG YLQQIAQAAD RLGFGGVLIP TGRSCEDSWL
VAASLIPVTQ RLKFLVALRP GIISPTVAAR QAATLDRLSN GRALFNLVTG GDPDELAGDG
LHLNHQERYE ASVEFTRIWR KVLEGEVVDY DGKHIQVKGA KLLYPPIQQP RPPLYFGGSS
EAAQDLAAEQ VELYLTWGEP PSAVAEKIAQ VREKAAAQGR EVRFGIRLHV IVRETNEEAW
AAADKLISHL DDDTIARAQA SLARFDSVGQ QRMAALHNGN RDKLEVSPNL WAGVGLVRGG
AGTALVGDGP TVAARVKEYA ELGIDTFIFS GYPHLEESYR VAELLFPHLD VQRPEQAKTS
GYVSPFGEMV ANDILPKSVA QS
