ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O85764

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name SSUD_PSEPU
Primary accession number O85764
Secondary accession numbers Q8KZQ8 Q9KHR0
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on January 10, 2003 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 42)
Name and origin of the protein
Protein name Alkanesulfonate monooxygenase
Synonyms EC 1.14.14.5
FMNH2-dependent aliphatic sulfonate monooxygenase
Gene name
Name: ssuD
Synonyms: dsuD
From
Pseudomonas putida [TaxID: 303] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DSM 6884 / S-313;
DOI=10.1128/JB.182.10.2869-2878.2000; PubMed=10781557 [NCBI, ExPASy, EBI, Israel, Japan]
Kahnert A., Vermeij P., Wietek C., James P., Leisinger T., Kertesz M.A.;
"The ssu locus plays a key role in organosulfur metabolism in Pseudomonas putida S-313.";
J. Bacteriol. 182:2869-2878(2000).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Rot18;
Kertesz M.A., Sialm M.;
"Sulfur-controlled aryl desulfonation phenotypes in Pseudomonas spp. and other soil isolates, and conservation of the sulfonate monooxygenase gene (ssuD).";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DS1;
DOI=10.1007/s00253-003-1233-7; PubMed=12835925 [NCBI, ExPASy, EBI, Israel, Japan]
Endoh T., Kasuga K., Horinouchi M., Yoshida T., Habe H., Nojiri H., Omori T.;
"Characterization and identification of genes essential for dimethyl sulfide utilization in Pseudomonas putida strain DS1.";
Appl. Microbiol. Biotechnol. 62:83-91(2003).
Comments
  • FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates. Seems also to be involved in the desulfurization of aromatic sulfonates.
  • CATALYTIC ACTIVITY: An alkanesufonate (R-CH2-SO3H) + FMNH2 + O2 = an aldehyde (R-CHO) + FMN + sulfite + H2O.
  • INDUCTION: Repressed by sulfate, cysteine, or thiocyanate.
  • MISCELLANEOUS: FMNH(2) which is absolutely required for this enzymatic reaction, is provided by ssuE.
  • SIMILARITY: Belongs to the ssuD family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF075709; AAC31905.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF250870; AAF81713.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB086390; BAC00973.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P80645; 1M41. [HSSP ENTRY / PDB]
SMR O85764; 1-355.
ModBase O85764.
Ontologies
GO
GO:0008726; Molecular function: alkanesulfonate monooxygenase activity (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01229; -; 1.
PBIL [Tree]
InterPro IPR011251; Luciferase-like_bac.
IPR016048; Luciferase_mOase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.30; Luciferase_like; 1.
Pfam PF00296; Bac_luciferase; 1.
Pfam graphical view of domain structure.
ProtoNet O85764.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
FMN; Monooxygenase; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   382  382     Alkanesulfonate monooxygenase. PRO_0000216713
CONFLICT   21    21        S -> N (in Ref. 2; AAF81713). 
CONFLICT   22    22        E -> D (in Ref. 1; AAC31905). 
CONFLICT   70    70        Q -> E (in Ref. 1; AAC31905). 
CONFLICT   95    95        L -> F (in Ref. 2; AAF81713). 
CONFLICT   147   147        V -> N (in Ref. 1; AAC31905). 
CONFLICT   167   167        I -> V (in Ref. 1; AAC31905). 
CONFLICT   181   181        E -> D (in Ref. 2; AAF81713). 
CONFLICT   202   202        S -> A (in Ref. 1 and 2). 
CONFLICT   221   221        E -> Q (in Ref. 2; AAF81713). 
CONFLICT   244   244        D -> E (in Ref. 2; AAF81713). 
CONFLICT   245   245        K -> R (in Ref. 1; AAC31905). 
CONFLICT   278   278        N -> G (in Ref. 1; AAC31905). 
CONFLICT   280   280        N -> K (in Ref. 2; AAF81713). 
CONFLICT   283   283        K -> N (in Ref. 1; AAC31905). 
CONFLICT   283   283        K -> Q (in Ref. 2; AAF81713). 
CONFLICT   321   321        E -> D (in Ref. 1; AAC31905). 
CONFLICT   349   349        L -> I (in Ref. 1; AAC31905). 
CONFLICT   356   356        Q -> I (in Ref. 2; AAF81713). 
CONFLICT   357   357        A -> P (in Ref. 1; AAC31905). 
CONFLICT   359   359        T -> S (in Ref. 2). 
CONFLICT   360   360        S -> G (in Ref. 1 and 2). 
CONFLICT   370   371        VA -> C (in Ref. 2; AAF81713). 
CONFLICT   380   380        A -> S (in Ref. 1; AAC31905). 
Sequence information
Length: 382 AA [This is the length of the unprocessed precursor] Molecular weight: 41553 Da [This is the MW of the unprocessed precursor] CRC64: B9117539DFF5DDAD [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSLNIFWFLP THGDGKYLGT SEGARAVDHG YLQQIAQAAD RLGFGGVLIP TGRSCEDSWL 

        70         80         90        100        110        120 
VAASLIPVTQ RLKFLVALRP GIISPTVAAR QAATLDRLSN GRALFNLVTG GDPDELAGDG 

       130        140        150        160        170        180 
LHLNHQERYE ASVEFTRIWR KVLEGEVVDY DGKHIQVKGA KLLYPPIQQP RPPLYFGGSS 

       190        200        210        220        230        240 
EAAQDLAAEQ VELYLTWGEP PSAVAEKIAQ VREKAAAQGR EVRFGIRLHV IVRETNEEAW 

       250        260        270        280        290        300 
AAADKLISHL DDDTIARAQA SLARFDSVGQ QRMAALHNGN RDKLEVSPNL WAGVGLVRGG 

       310        320        330        340        350        360 
AGTALVGDGP TVAARVKEYA ELGIDTFIFS GYPHLEESYR VAELLFPHLD VQRPEQAKTS 

       370        380 
GYVSPFGEMV ANDILPKSVA QS
O85764 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!