Reviewed,
UniProtKB/Swiss-Prot P37337 (BPHG_BURXL)
Last modified
November 3, 2009.
Version 62.
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: Biphenyl dioxygenase system ferredoxin--NAD(+) reductase component EC=1.18.1.3 | ||||||
| Gene names |
| ||||||
| Organism | Burkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 266265 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia |
Protein attributes
| Sequence length | 408 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Part of the electron transfer component of biphenyl dioxygenase, transfers electrons from ferredoxin (bphF) to NADH. |
| Catalytic activity | Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH. |
| Cofactor | FAD. |
| Pathway | |
| Subunit structure | This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (bphA and bphE), a ferredoxin (bphF) and a ferredoxin reductase (bphG). |
| 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 | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW cell redox homeostasisInferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro ferredoxin-NAD+ reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequencing and transcriptional mapping of the genes encoding biphenyl dioxygenase, a multicomponent polychlorinated-biphenyl-degrading enzyme in Pseudomonas strain LB400." Erickson B.D., Mondello F.J. J. Bacteriol. 174:2903-2912(1992) [PubMed: 1569021] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | Erickson B.D., Mondello F.J. Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [3] | "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome shaped for versatility." Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., Parnell J.J. Tiedje J.M.Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006) [PubMed: 17030797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| M86348 Genomic DNA. Translation: AAB63429.1. CP000272 Genomic DNA. Translation: ABE37055.1. | |
| PIR | F41858. |
| RefSeq | YP_556405.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1D7Y based on UniProtKB Q52437. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4010705. |
| GenomeReviews | Gene locus Bxeno_C1127 in contig CP000272_GR. |
| KEGG | bxe:Bxe_C1193. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P37337. |
| OMA | CEVATTA. |
Enzyme and pathway databases | |
| BioCyc | BXEN266265:BXE_C1193-MON. |
Family and domain databases | |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR001327. Pyr_OxRdtase_NAD_bd. [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. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | BPHG_BURXL | ||||||||
| Accession | Primary (citable) accession number: P37337 Secondary accession number(s): Q13FT4 | ||||||||
| 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


