Reviewed,
UniProtKB/Swiss-Prot O67987 (CLCA_RHOOP)
Last modified
February 9, 2010.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Chlorocatechol 1,2-dioxygenase EC=1.13.11.- | ||
| Gene names |
| ||
| Organism | Rhodococcus opacus (Nocardia opaca) | ||
| Taxonomic identifier | 37919 [NCBI] | ||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus |
Protein attributes
| Sequence length | 257 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 4-chlorocatechol + O2 = 3-chloro-muconate. 3,5-dichlorocatechol + O2 = 2,4-dichloro -muconate. |
| Cofactor | Binds 1 Fe3+ 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 | 3D-structure |
| 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 chlorocatechol 1,2-dioxygenase activityInferred 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 – 257 | 257 | Chlorocatechol 1,2-dioxygenase | PRO_0000085088 | ||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||
| Metal binding | 134 | 1 | Iron By similarity | |||||||||||||||||||||||||||||||||||||
| Metal binding | 169 | 1 | Iron By similarity | |||||||||||||||||||||||||||||||||||||
| Metal binding | 194 | 1 | Iron By similarity | |||||||||||||||||||||||||||||||||||||
| Metal binding | 196 | 1 | Iron By similarity | |||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||
| Helix | 4 – 24 | 21 | ||||||||||||||||||||||||||||||||||||||
| Helix | 28 – 43 | 16 | ||||||||||||||||||||||||||||||||||||||
| Helix | 47 – 54 | 8 | ||||||||||||||||||||||||||||||||||||||
| Helix | 56 – 63 | 8 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 67 – 69 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 103 – 112 | 10 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 122 – 126 | 5 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 147 – 151 | 5 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 157 – 164 | 8 | ||||||||||||||||||||||||||||||||||||||
| Helix | 176 – 182 | 7 | ||||||||||||||||||||||||||||||||||||||
| Turn | 183 – 185 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 194 – 201 | 8 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 204 – 213 | 10 | ||||||||||||||||||||||||||||||||||||||
| Turn | 217 – 220 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 229 – 231 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 246 – 254 | 9 | ||||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Evolutionary relationship between chlorocatechol catabolic enzymes from Rhodococcus opacus 1CP and their counterparts in proteobacteria: sequence divergence and functional convergence." Eulberg D., Kourbatova E.M., Golovleva L.A., Schloemann M. J. Bacteriol. 180:1082-1094(1998) [PubMed: 9495745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 1CP. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF003948 Genomic DNA. Translation: AAC38251.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ModBase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR007535. Catechol_dOase_N. IPR012817. Chlorcchol_dOase. 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 | TIGR02465. chlorocat_1_2. 1 hit. | ||||||||||||
| PROSITE | PS00083. INTRADIOL_DIOXYGENAS. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | CLCA_RHOOP | ||||||||
| Accession | Primary (citable) accession number: O67987 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


