Q0K9I0 (SSUD_CUPNH) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 45.
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 | Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 381666 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus |
Protein attributes
| Sequence length | 387 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the desulfonation of aliphatic sulfonates By similarity. HAMAP MF_01229 |
| Catalytic activity | An alkanesufonate (R-CH(2)-SO3H) + FMNH2 + O2 = an aldehyde (R-CHO) + FMN + sulfite + H2O. HAMAP MF_01229 |
| Sequence similarities | Belongs to the SsuD family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | FMN |
| Molecular function | Monooxygenase Oxidoreductase |
| Technical term | Complete proteome |
| 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 – 387 | 387 | Alkanesulfonate monooxygenase HAMAP MF_01229 | PRO_1000066832 | |||
Sequences
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References
| [1] | "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16." Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B. Nat. Biotechnol. 24:1257-1262(2006) [PubMed: 16964242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM260479 Genomic DNA. Translation: CAJ93341.1. |
| RefSeq | YP_726709.1. NC_008313.1. |
3D structure databases | |
| ProteinModelPortal | Q0K9I0. |
| SMR | Q0K9I0. Positions 1-355. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q0K9I0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4250093. |
| GenomeReviews | Gene locus H16_A2244 in contig AM260479_GR. |
| KEGG | reh:H16_A2244. |
| PATRIC | 35234003. VBIRalEut6770_2649. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2141. |
| HOGENOM | HBG639644. |
| OMA | HASHSER. |
| PhylomeDB | Q0K9I0. |
| ProtClustDB | PRK00719. |
Enzyme and pathway databases | |
| BioCyc | REUT381666:H16_A2244-MONOMER. |
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. |
| KO | K04091. |
| 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_CUPNH | ||||||||
| Accession | Primary (citable) accession number: Q0K9I0 | ||||||||
| 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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