Reviewed,
UniProtKB/Swiss-Prot Q8KN28 (TFDB_DELAC)
Last modified
March 24, 2009.
Version 37.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 2,4-dichlorophenol 6-monooxygenase EC=1.14.13.20 Alternative name(s): 2,4-dichlorophenol hydroxylase Short name=2,4-DCP hydroxylase | ||
| Gene names |
| ||
| Organism | Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans) | ||
| Taxonomic identifier | 80866 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Delftia |
Protein attributes
| Sequence length | 586 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Transforms 2,4-dichlorophenol (2,4-DCP) into 3,5-dichlorocatechol By similarity. UniProtKB P27138 |
| Catalytic activity | 2,4-dichlorophenol + NADPH + O2 = 3,5-dichlorocatechol + NADP+ + H2O. UniProtKB P27138 |
| Cofactor | FAD By similarity. UniProtKB P27138 |
| Pathway | Xenobiotic degradation; 2,4-dichlorophenoxyacetic acid degradation. |
| Subunit structure | Homotetramer By similarity. UniProtKB P27138 |
| Sequence similarities | Belongs to the pheA/tfdB FAD monooxygenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Monooxygenase Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 2,4-dichlorophenol 6-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 – 586 | 586 | 2,4-dichlorophenol 6-monooxygenase | PRO_0000214050 | |||||
Regions | |||||||||
| Nucleotide binding | 11 – 40 | 30 | FAD Potential | ||||||
| Nucleotide binding | 304 – 314 | 11 | FAD Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 2 | 1 | Missing AA sequence Ref.4 | ||||||
| Sequence conflict | 18 | 1 | G → A AA sequence Ref.4 | ||||||
| Sequence conflict | 195 | 1 | M → V in AAD55079. Ref.3 | ||||||
Sequences
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References
| [1] | "A transposon encoding the complete 2,4-dichlorophenoxyacetic acid degradation pathway in the alkalitolerant strain Delftia acidovorans P4a." Hoffmann D., Kleinsteuber S., Mueller R.H., Babel W. Microbiology 149:2545-2556(2003) [PubMed: 12949179] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: P4a. |
| [2] | "Development and application of PCR primers for the detection of the tfd genes in Delftia acidovorans P4a involved in the degradation of 2,4-D." Hoffmann D., Kleinsteuber S., Mueller R.H., Babel W. Acta Biotechnol. 21:321-331(2001) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 57-434. Strain: P4a. |
| [3] | "Physiological and genetic characteristics of two bacterial strains utilizing phenoxypropionate and phenoxyacetate herbicides." Mueller R.H., Kleinsteuber S., Babel W. Microbiol. Res. 156:121-131(2001) [PubMed: 11572451] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-432. Strain: MC1. |
| [4] | "Regulation of catabolic enzymes during long-term exposure of Delftia acidovorans MC1 to chlorophenoxy herbicides." Benndorf D., Davidson I., Babel W. Microbiology 150:1005-1014(2004) [PubMed: 15073309] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-19. Strain: MC1. |
Cross-references
Sequence databases | |
|---|---|
| AY078159 Genomic DNA. Translation: AAM76774.1. AF176242 Genomic DNA. Translation: AAD55079.1. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.14.13.20. 140899. |
Family and domain databases | |
| InterPro | IPR002938. mOase_FAD_bd. IPR003042. Rng_hydrolase-like. [Graphical view] |
| Pfam | PF01494. FAD_binding_3. 1 hit. [Graphical view] |
| PRINTS | PR00420. RNGMNOXGNASE. |
| ProtoNet | Search... |
Entry information
| Entry name | TFDB_DELAC | ||||||||
| Accession | Primary (citable) accession number: Q8KN28 Secondary accession number(s): Q93T15, Q9RP01 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


