Reviewed,
UniProtKB/Swiss-Prot P0C618 (BNZA_PSEPU)
Last modified
January 19, 2010.
Version 12.
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: Benzene 1,2-dioxygenase subunit alpha EC=1.14.12.3 Alternative name(s): Benzene 1,2-dioxygenase P1 subunit Toluene 2,3-dioxygenase subunit alpha EC=1.14.12.11 | ||||
| Gene names |
| ||||
| Organism | Pseudomonas putida | ||||
| Taxonomic identifier | 303 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 450 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes both the oxidation of benzene and toluene. |
| Catalytic activity | Benzene + NADH + O2 = cis-cyclohexa-3,5-diene-1,2-diol + NAD+. Toluene + NADH + O2 = (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+. |
| Cofactor | Binds 1 2Fe-2S cluster per subunit By similarity. Binds 1 iron ion per subunit By similarity. |
| Pathway | Aromatic compound metabolism; benzene degradation; catechol from benzene: step 1/2. |
| Subunit structure | This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (bnzA and bnzB), a ferredoxin (bnzC) and a ferredoxin reductase (bnzD). |
| Sequence similarities | Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family. Contains 1 Rieske domain. |
| Sequence caution | The sequence AAA25735.1 differs from that shown. Reason: Frameshift at positions 330, 339, 360, 362, 368 and 393. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | 2Fe-2S Iron Iron-sulfur Metal-binding NAD |
| Molecular function | Dioxygenase Oxidoreductase |
| 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 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW benzene 1,2-dioxygenase activityInferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygenInferred from electronic annotation. Source: UniProtKB-KW toluene dioxygenase activityInferred 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 – 450 | 450 | Benzene 1,2-dioxygenase subunit alpha | PRO_0000085045 | |||||
Regions | |||||||||
| Domain | 54 – 163 | 110 | Rieske | ||||||
Sites | |||||||||
| Metal binding | 96 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 98 | 1 | Iron-sulfur (2Fe-2S); via pros nitrogen By similarity | ||||||
| Metal binding | 116 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 119 | 1 | Iron-sulfur (2Fe-2S); via pros nitrogen By similarity | ||||||
| Metal binding | 222 | 1 | Iron By similarity | ||||||
| Metal binding | 228 | 1 | Iron By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Nucleotide sequencing and characterization of the genes encoding benzene oxidation enzymes of Pseudomonas putida." Irie S., Doi S., Yorifuji T., Takagi M., Yano K. J. Bacteriol. 169:5174-5179(1987) [PubMed: 3667527] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BE-81. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M17904 Genomic DNA. Translation: AAA25735.1. Frameshift. |
| PIR | A29830. |
3D structure databases | |
| SMR | P0C618. Positions 15-450. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.14.12.11. 403. 1.14.12.3. 403. |
Family and domain databases | |
| InterPro | IPR017941. Rieske_2Fe-2S. IPR015881. Ring-hydroxy_dOase_2Fe2S_BS. IPR015879. Ring_hydroxy_dOase_asu_C. IPR001663. Rng_hydr_dOase-A. [Graphical view] |
| PANTHER | PTHR21266:SF2. Rng_hydr_dOase-A. 1 hit. |
| Pfam | PF00355. Rieske. 1 hit. PF00848. Ring_hydroxyl_A. 1 hit. [Graphical view] |
| PRINTS | PR00090. RNGDIOXGNASE. |
| PROSITE | PS51296. RIESKE. 1 hit. PS00570. RING_HYDROXYL_ALPHA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | BNZA_PSEPU | ||||||||
| Accession | Primary (citable) accession number: P0C618 Secondary accession number(s): P08084, P13450 | ||||||||
| Entry history |
| ||||||||
| 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


