O85764 (SSUD_PSEPU) Reviewed, UniProtKB/Swiss-Prot
Last modified
July 27, 2011.
Version 58.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Alkanesulfonate monooxygenase EC=1.14.14.5 Alternative name(s): FMNH2-dependent aliphatic sulfonate monooxygenase | ||||
| Gene names |
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| Organism | Pseudomonas putida (Arthrobacter siderocapsulatus) | ||||
| Taxonomic identifier | 303 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 382 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Catalyzes the desulfonation of aliphatic sulfonates. Seems also to be involved in the desulfurization of aromatic sulfonates. HAMAP MF_01229 |
| Catalytic activity | An alkanesufonate (R-CH(2)-SO3H) + FMNH2 + O2 = an aldehyde (R-CHO) + FMN + sulfite + H2O. HAMAP MF_01229 |
| Induction | Repressed by sulfate, cysteine, or thiocyanate. HAMAP MF_01229 |
| Miscellaneous | FMNH2 which is absolutely required for this enzymatic reaction, is provided by SsuE. HAMAP MF_01229 |
| Sequence similarities | Belongs to the SsuD family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | FMN |
| Molecular function | Monooxygenase Oxidoreductase |
| Gene Ontology (GO) | |
| Molecular function | alkanesulfonate monooxygenase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 382 | 382 | Alkanesulfonate monooxygenase HAMAP MF_01229 | PRO_0000216713 | |||||
Experimental info | |||||||||
| Sequence conflict | 21 | 1 | S → N in AAF81713. Ref.2 | ||||||
| Sequence conflict | 22 | 1 | E → D in AAC31905. Ref.1 | ||||||
| Sequence conflict | 70 | 1 | Q → E in AAC31905. Ref.1 | ||||||
| Sequence conflict | 95 | 1 | L → F in AAF81713. Ref.2 | ||||||
| Sequence conflict | 147 | 1 | V → N in AAC31905. Ref.1 | ||||||
| Sequence conflict | 167 | 1 | I → V in AAC31905. Ref.1 | ||||||
| Sequence conflict | 181 | 1 | E → D in AAF81713. Ref.2 | ||||||
| Sequence conflict | 202 | 1 | S → A Ref.1 | ||||||
| Sequence conflict | 202 | 1 | S → A Ref.2 | ||||||
| Sequence conflict | 221 | 1 | E → Q in AAF81713. Ref.2 | ||||||
| Sequence conflict | 244 | 1 | D → E in AAF81713. Ref.2 | ||||||
| Sequence conflict | 245 | 1 | K → R in AAC31905. Ref.1 | ||||||
| Sequence conflict | 278 | 1 | N → G in AAC31905. Ref.1 | ||||||
| Sequence conflict | 280 | 1 | N → K in AAF81713. Ref.2 | ||||||
| Sequence conflict | 283 | 1 | K → N in AAC31905. Ref.1 | ||||||
| Sequence conflict | 283 | 1 | K → Q in AAF81713. Ref.2 | ||||||
| Sequence conflict | 321 | 1 | E → D in AAC31905. Ref.1 | ||||||
| Sequence conflict | 349 | 1 | L → I in AAC31905. Ref.1 | ||||||
| Sequence conflict | 356 | 1 | Q → I in AAF81713. Ref.2 | ||||||
| Sequence conflict | 357 | 1 | A → P in AAC31905. Ref.1 | ||||||
| Sequence conflict | 359 | 1 | T → S Ref.2 | ||||||
| Sequence conflict | 360 | 1 | S → G Ref.1 | ||||||
| Sequence conflict | 360 | 1 | S → G Ref.2 | ||||||
| Sequence conflict | 370 – 371 | 2 | VA → C in AAF81713. Ref.2 | ||||||
| Sequence conflict | 380 | 1 | A → S in AAC31905. Ref.1 | ||||||
Sequences
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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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF075709 Genomic DNA. Translation: AAC31905.1. AF250870 Genomic DNA. Translation: AAF81713.1. AB086390 Genomic DNA. Translation: BAC00973.1. |
3D structure databases | |
| ProteinModelPortal | O85764. |
| SMR | O85764. Positions 1-355. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-14252. |
Family and domain databases | |
| HAMAP | MF_01229. Alkanesulf_monooxygen. [Tree] |
| InterPro | IPR019911. Alkanesulphonate_mOase_FMN-dep. IPR011251. Luciferase-like_dom. [Graphical view] |
| Gene3D | G3DSA:3.20.20.30. Luciferase_like. 2 hits. |
| Pfam | PF00296. Bac_luciferase. 1 hit. [Graphical view] |
| SUPFAM | SSF51679. Luciferase_like. 1 hit. |
| TIGRFAMs | TIGR03565. Alk_sulf_monoox. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | SSUD_PSEPU | ||||||||
| Accession | Primary (citable) accession number: O85764 Secondary accession number(s): Q8KZQ8, Q9KHR0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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