ID   SSUD_PSE14              Reviewed;         379 AA.
AC   Q48H03;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Alkanesulfonate monooxygenase;
DE            EC=1.14.14.5;
DE   AltName: Full=FMNH2-dependent aliphatic sulfonate monooxygenase;
GN   Name=ssuD; OrderedLocusNames=PSPPH_3167;
OS   Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L.,
RA   Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O.,
RA   Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D.,
RA   Mansfield J.W., Collmer A., Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv.
RT   phaseolicola 1448A reveals divergence among pathovars in genes
RT   involved in virulence and transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
CC   -!- FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: An alkanesufonate (R-CH(2)-SO(3)H) + FMNH(2) +
CC       O(2) = an aldehyde (R-CHO) + FMN + sulfite + H(2)O.
CC   -!- SIMILARITY: Belongs to the ssuD family.
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DR   EMBL; CP000058; AAZ34006.1; -; Genomic_DNA.
DR   RefSeq; YP_275330.1; -.
DR   SMR; Q48H03; 1-347.
DR   GeneID; 3556547; -.
DR   GenomeReviews; CP000058_GR; PSPPH_3167.
DR   KEGG; psp:PSPPH_3167; -.
DR   NMPDR; fig|264730.3.peg.3104; -.
DR   HOGENOM; Q48H03; -.
DR   OMA; Q48H03; GGDPVEN.
DR   GO; GO:0008726; F:alkanesulfonate monooxygenase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01229; -; 1.
DR   InterPro; IPR019911; Alkanesulfonate_mOase_FMN-dep.
DR   InterPro; IPR011251; Luciferase-like.
DR   InterPro; IPR016048; Luciferase-like_sub.
DR   Gene3D; G3DSA:3.20.20.30; Luciferase_like; 1.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   TIGRFAMs; TIGR03565; Alk_sulf_monoox; 1.
PE   3: Inferred from homology;
KW   Complete proteome; FMN; Monooxygenase; Oxidoreductase.
FT   CHAIN         1    379       Alkanesulfonate monooxygenase.
FT                                /FTId=PRO_1000066827.
SQ   SEQUENCE   379 AA;  41510 MW;  C46975AE057E7E5D CRC64;
     MNVFWFLPTH GDGHYLGTTK GARPVTLNYL KQVAQAADDL GYYGVLIPTG RSCEDSWVIA
     SALVPLTERL KYLVAIRPGI ISPTVSARMA ATLDRLSGGR LLINVVTGGD PDENRGDGSF
     LDHSERYEVT DEFLKIWRRV LQGEAVDFEG KHLRVQNAKA LYPPIQKPYP PLYFGGSSDA
     AHDLAADQVD VYLTWGEPPA AVAQKLADVR ERAARKGRTV KFGIRLHVIV RETSEEAWKA
     ASTLIEHISD ETIAAAQKSF SRFDSEGQRR MAALHDGRRD NLEIAPNLWA GVGLVRGGAG
     TALVGNPQEV AARIKEYADL GIDSFIFSGY PHLEEAYRFA ELVFPLLPEP YASLAGRGIT
     NLTGPFGEMI ANDLPPQAK
//