ID   SSUD_PSEU2              Reviewed;         379 AA.
AC   Q4ZRE3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Psyr_3247;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY38279.1; -; Genomic_DNA.
DR   RefSeq; WP_011268305.1; NC_007005.1.
DR   RefSeq; YP_236317.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZRE3; -.
DR   SMR; Q4ZRE3; -.
DR   STRING; 205918.Psyr_3247; -.
DR   EnsemblBacteria; AAY38279; AAY38279; Psyr_3247.
DR   KEGG; psb:Psyr_3247; -.
DR   PATRIC; fig|205918.7.peg.3317; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_0_6; -.
DR   OMA; YGFWLPI; -.
DR   Proteomes; UP000000426; 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.
FT   CHAIN           1..379
FT                   /note="Alkanesulfonate monooxygenase"
FT                   /id="PRO_1000066831"
SQ   SEQUENCE   379 AA;  41539 MW;  8474E505D025F22F CRC64;
     MNVFWFLPTH GDGHYLGTTK GARPVTLNYL KQVAQAADDL GYYGVLIPTG RSCEDSWVIA
     SALVPLTERL RYLVAIRPGI ISPTVSARMA ATLDRLSGGR LLINVVTGGD PDENRGDGSF
     LDHSERYEVT DEFLKIWRRV LQGEAVDFEG KHLRVQNAKA LYPPIQQPYP PLYFGGSSDA
     AHDLAADQVD VYLTWGEPPA AVAQKLADVR ERAARKGRTV KFGIRLHVIV RETSEEAWKA
     ASTLIEHISD DTIAAAQKSF SRFDSEGQRR MAALHDGRRD NLEIAPNLWA GVGLVRGGAG
     TALVGNPEEV AARIKEYADL GIESFIFSGY PHLEEAYRFA ELVFPLLPEP YASLAGRGIT
     NLTGPFGEMI ANDLPPQAK