Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot O85764 (SSUD_PSEPU)

Last modified November 4, 2008. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Alkanesulfonate monooxygenase
    EC=1.14.14.5
Alternative name(s):
    FMNH2-dependent aliphatic sulfonate monooxygenase
Gene names
Name: ssuD
Synonyms: dsuD
OrganismPseudomonas putida
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Hide | Top

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

Hide | Top

General annotation (Comments)

Function

Catalyzes the desulfonation of aliphatic sulfonates. Seems also to be involved in the desulfurization of aromatic sulfonates.

Catalytic activity

An alkanesufonate (R-CH(2)-SO(3)H) + FMNH(2) + O(2) = an aldehyde (R-CHO) + FMN + sulfite + H(2)O.

Induction

Repressed by sulfate, cysteine, or thiocyanate.

Miscellaneous

FMNH(2) which is absolutely required for this enzymatic reaction, is provided by ssuE.

Sequence similarities

Belongs to the ssuD family.

Hide | Top

Ontologies

Keywords

   LigandFMN
   Molecular functionMonooxygenase
Oxidoreductase

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalkanesulfonate monooxygenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Alkanesulfonate monooxygenase
PRO_0000216713

Experimental info

Sequence conflict211S → N in AAF81713. Ref.2
Sequence conflict221E → D in AAC31905. Ref.1
Sequence conflict701Q → E in AAC31905. Ref.1
Sequence conflict951L → F in AAF81713. Ref.2
Sequence conflict1471V → N in AAC31905. Ref.1
Sequence conflict1671I → V in AAC31905. Ref.1
Sequence conflict1811E → D in AAF81713. Ref.2
Sequence conflict2021S → A Ref.1 Ref.2
Sequence conflict2211E → Q in AAF81713. Ref.2
Sequence conflict2441D → E in AAF81713. Ref.2
Sequence conflict2451K → R in AAC31905. Ref.1
Sequence conflict2781N → G in AAC31905. Ref.1
Sequence conflict2801N → K in AAF81713. Ref.2
Sequence conflict2831K → N in AAC31905. Ref.1
Sequence conflict2831K → Q in AAF81713. Ref.2
Sequence conflict3211E → D in AAC31905. Ref.1
Sequence conflict3491L → I in AAC31905. Ref.1
Sequence conflict3561Q → I in AAF81713. Ref.2
Sequence conflict3571A → P in AAC31905. Ref.1
Sequence conflict3591T → S Ref.2
Sequence conflict3601S → G Ref.1 Ref.2
Sequence conflict370 – 3712VA → C in AAF81713. Ref.2
Sequence conflict3801A → S in AAC31905. Ref.1

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
O85764-1 [UniParc].

Last modified January 10, 2003. Version 2.
Checksum: B9117539DFF5DDAD

FASTA38241,553
        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

« Hide

Hide | Top

References

[1]"The ssu locus plays a key role in organosulfur metabolism in Pseudomonas putida S-313."
Kahnert A., Vermeij P., Wietek C., James P., Leisinger T., Kertesz M.A.
J. Bacteriol. 182:2869-2878(2000) [PubMed: 10781557] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 6884 / S-313.
[2]"Sulfur-controlled aryl desulfonation phenotypes in Pseudomonas spp. and other soil isolates, and conservation of the sulfonate monooxygenase gene (ssuD)."
Kertesz M.A., Sialm M.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Rot18.
[3]"Characterization and identification of genes essential for dimethyl sulfide utilization in Pseudomonas putida strain DS1."
Endoh T., Kasuga K., Horinouchi M., Yoshida T., Habe H., Nojiri H., Omori T.
Appl. Microbiol. Biotechnol. 62:83-91(2003) [PubMed: 12835925] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DS1.

Hide | Top

Cross-references

Sequence databases

AF075709 Genomic DNA. Translation: AAC31905.1.
AF250870 Genomic DNA. Translation: AAF81713.1.
AB086390 Genomic DNA. Translation: BAC00973.1.

3D structure databases

HSSPHSSP built from PDB template 1M41 based on UniProtKB P80645.
SMRO85764. Positions 1-355.
ModBaseSearch...

Family and domain databases

HAMAPMF_01229.
[Tree]
InterProIPR011251. Luciferase-like_bac.
IPR016048. Luciferase_mOase.
[Graphical view]
Gene3DG3DSA:3.20.20.30. Luciferase_like. 1 hit.
PfamPF00296. Bac_luciferase. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameSSUD_PSEPU
AccessionPrimary (citable) accession number: O85764
Secondary accession number(s): Q8KZQ8, Q9KHR0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 10, 2003
Last modified: November 4, 2008
This is version 42 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents