Q46373 (BPHE_COMTE) Reviewed, UniProtKB/Swiss-Prot
Last modified
June 28, 2011.
Version 55.
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: Biphenyl dioxygenase subunit beta EC=1.14.12.18 Alternative name(s): Biphenyl 2,3-dioxygenase | ||
| Gene names |
| ||
| Organism | Comamonas testosteroni (Pseudomonas testosteroni) | ||
| Taxonomic identifier | 285 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Comamonas |
Protein attributes
| Sequence length | 186 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | The beta subunit may be responsible for the substrate specificity of the enzyme. |
| Catalytic activity | Biphenyl + NADH + O2 = (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+. |
| Pathway | |
| Subunit structure | Heterohexamer consisting of 3 BphA subunits and 3 BphE subunits. A ferredoxin (BphF) and a ferredoxin reductase (BphG) must be present to obtain activity. |
| Sequence similarities | Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | NAD |
| Molecular function | Dioxygenase Oxidoreductase |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | biphenyl 2,3-dioxygenase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygenInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 186 | 186 | Biphenyl dioxygenase subunit beta | PRO_0000085069 | ||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||
| Helix | 19 – 37 | 19 | ||||||||||||||||||||||||||||||||||||
| Helix | 41 – 45 | 5 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 48 – 57 | 10 | ||||||||||||||||||||||||||||||||||||
| Helix | 64 – 66 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 78 – 82 | 5 | ||||||||||||||||||||||||||||||||||||
| Helix | 84 – 87 | 4 | ||||||||||||||||||||||||||||||||||||
| Helix | 91 – 94 | 4 | ||||||||||||||||||||||||||||||||||||
| Turn | 95 – 97 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 100 – 102 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 107 – 119 | 13 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 126 – 138 | 13 | ||||||||||||||||||||||||||||||||||||
| Turn | 139 – 141 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 142 – 146 | 5 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 150 – 155 | 6 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 164 – 170 | 7 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 175 – 177 | 3 | ||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Sequencing of Comamonas testosteroni strain B-356-biphenyl/chlorobiphenyl dioxygenase genes: evolutionary relationships among Gram-negative bacterial biphenyl dioxygenases." Sylvestre M., Sirois M., Hurtubise Y., Bergeron J., Ahmad D., Shareck F., Barriault D., Guillemette I., Juteau J.-M. Gene 174:195-202(1996) [PubMed: 8890734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B-356. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U47637 Genomic DNA. Translation: AAC44527.1. | ||||||||||||||||||
| PIR | JC4994. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | Q46373. | ||||||||||||||||||
| SMR | Q46373. Positions 6-186. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR000391. Rng_hydr_dOase-bsu. [Graphical view] | ||||||||||||||||||
| Pfam | PF00866. Ring_hydroxyl_B. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | BPHE_COMTE | ||||||||
| Accession | Primary (citable) accession number: Q46373 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with