Reviewed,
UniProtKB/Swiss-Prot P95607 (CATA_RHOOP)
Last modified
November 25, 2008.
Version 43.
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
Names and origin
| Protein names | Recommended name: Catechol 1,2-dioxygenase EC=1.13.11.1 Alternative name(s): 1,2-CTD | ||
| Gene names |
| ||
| Organism | Rhodococcus opacus (Nocardia opaca) | ||
| Taxonomic identifier | 37919 [NCBI] | ||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus |
Protein attributes
| Sequence length | 270 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Catechol + O(2) = cis,cis-muconate. |
| Cofactor | Binds 1 Fe(3+) ion per subunit. |
| Sequence similarities | Belongs to the intradiol ring-cleavage dioxygenase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | Iron Metal-binding |
| Molecular function | Dioxygenase Oxidoreductase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW catechol metabolic processInferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | catechol 1,2-dioxygenase activity Inferred from electronic annotation. Source: InterPro ferric iron bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – 270 | ›270 | Catechol 1,2-dioxygenase | PRO_0000085084 | |||||
Sites | |||||||||
| Metal binding | 152 | 1 | Iron By similarity | ||||||
| Metal binding | 186 | 1 | Iron By similarity | ||||||
| Metal binding | 210 | 1 | Iron By similarity | ||||||
| Metal binding | 212 | 1 | Iron By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Characterization of catechol catabolic genes from Rhodococcus erythropolis 1CP." Eulberg D., Golovleva L.A., Schloemann M. J. Bacteriol. 179:370-381(1997) [PubMed: 8990288] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 113-132 AND 195-203. Strain: 1CP. |
Cross-references
Sequence databases | |
|---|---|
| X99622 Genomic DNA. Translation: CAA67941.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1DMH based on UniProtKB P07773. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR007535. Catechol_dOase_N. IPR012800. Cchol_dOase_actb. IPR000627. Intradiol_dOase_C. IPR015889. Intradiol_dOase_core. [Graphical view] |
| Gene3D | G3DSA:2.60.130.10. Intradiol_dOase_core. 1 hit. |
| Pfam | PF00775. Dioxygenase_C. 1 hit. PF04444. Dioxygenase_N. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02438. catachol_actin. 1 hit. |
| PROSITE | PS00083. INTRADIOL_DIOXYGENAS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CATA_RHOOP | ||||||||
| Accession | Primary (citable) accession number: P95607 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


