Q07946 (BEDA_PSEPU) Reviewed, UniProtKB/Swiss-Prot
Last modified
June 28, 2011.
Version 69.
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: Benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit EC=1.18.1.3 | ||
| Gene names |
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| Encoded on | Plasmid pHMT112 | ||
| Organism | Pseudomonas putida (Arthrobacter siderocapsulatus) | ||
| Taxonomic identifier | 303 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 410 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Part of the electron transfer component of benzene 1,2-dioxygenase, transfers electrons from ferredoxin to NADH. |
| Catalytic activity | Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH. |
| Cofactor | FAD. |
| 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 (BedC1 and BedC2), a ferredoxin (BedB) and a ferredoxin reductase (BedA). |
| Sequence similarities | Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | FAD Flavoprotein NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing Plasmid |
| Gene Ontology (GO) | |
| Biological process | aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW cell redox homeostasisInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | ferredoxin-NAD+ reductase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The Pseudomonas putida ML2 plasmid-encoded genes for benzene dioxygenase are unusual in codon usage and low in G+C content." Tan H.-M., Tang H.-Y., Joannou C., Abdel-Wahab N.H., Mason J.R. Gene 130:33-39(1993) [PubMed: 8344526] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-14. Strain: ML2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF148496 Genomic DNA. Translation: AAA17761.1. |
| PIR | JN0810. |
3D structure databases | |
| ProteinModelPortal | Q07946. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-12882. |
Family and domain databases | |
| InterPro | IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit. |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. |
| SUPFAM | SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | BEDA_PSEPU | ||||||||
| Accession | Primary (citable) accession number: Q07946 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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