Reviewed,
UniProtKB/Swiss-Prot P37332 (BPHF_BURXL)
Last modified
June 16, 2009.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Biphenyl dioxygenase system ferredoxin subunit | ||||||
| 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 | 109 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This protein seems to be a 2Fe-2S ferredoxin. |
| 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 component family. Contains 1 Rieske domain. |
| biophysicochemical properties | Redox potential: E0 is -157 mV. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism Electron transport Transport |
| Ligand | 2Fe-2S Iron Iron-sulfur Metal-binding |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW electron transport chainInferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activityInferred 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 – 109 | 109 | Biphenyl dioxygenase system ferredoxin subunit | PRO_0000201686 | |||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||
| Domain | 4 – 100 | 97 | Rieske | ||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||
| Metal binding | 43 | 1 | Iron-sulfur (2Fe-2S) | ||||||||||||||||||||||||||||||
| Metal binding | 45 | 1 | Iron-sulfur (2Fe-2S); via pros nitrogen | ||||||||||||||||||||||||||||||
| Metal binding | 63 | 1 | Iron-sulfur (2Fe-2S) | ||||||||||||||||||||||||||||||
| Metal binding | 66 | 1 | Iron-sulfur (2Fe-2S); via pros nitrogen | ||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||
| Beta strand | 4 – 8 | 5 | |||||||||||||||||||||||||||||||
| Helix | 9 – 11 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 17 – 22 | 6 | |||||||||||||||||||||||||||||||
| Beta strand | 25 – 32 | 8 | |||||||||||||||||||||||||||||||
| Beta strand | 35 – 42 | 8 | |||||||||||||||||||||||||||||||
| Beta strand | 49 – 51 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 60 – 62 | 3 | |||||||||||||||||||||||||||||||
| Turn | 64 – 66 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 69 – 71 | 3 | |||||||||||||||||||||||||||||||
| Turn | 72 – 74 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 77 – 81 | 5 | |||||||||||||||||||||||||||||||
| Beta strand | 91 – 94 | 4 | |||||||||||||||||||||||||||||||
| Beta strand | 97 – 100 | 4 | |||||||||||||||||||||||||||||||
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]. |
| [4] | "Characterization of BphF, a Rieske-type ferredoxin with a low reduction potential." Couture M.M.-J., Colbert C.L., Babini E., Rosell F.I., Mauk A.G., Bolin J.T., Eltis L.D. Biochemistry 40:84-92(2001) [PubMed: 11141059] [Abstract] Cited for: CHARACTERIZATION. |
| [5] | "A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins." Colbert C.L., Couture M.M.-J., Eltis L.D., Bolin J.T. Structure 8:1267-1278(2000) [PubMed: 11188691] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M86348 Genomic DNA. Translation: AAB63428.1. CP000272 Genomic DNA. Translation: ABE37056.1. | |||||||||||||
| PIR | E41858. | ||||||||||||
| RefSeq | YP_556406.1. | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 4010706. | ||||||||||||
| GenomeReviews | Gene locus Bxeno_C1128 in contig CP000272_GR. | ||||||||||||
| KEGG | bxe:Bxe_C1194. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P37332. | ||||||||||||
| OMA | P37332. ECWAHGS. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | BXEN266265:BXE_C1194-MON. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR017941. Rieske_2Fe-2S. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:2.102.10.10. Rieske_reg. 1 hit. | ||||||||||||
| Pfam | PF00355. Rieske. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS51296. RIESKE. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | BPHF_BURXL | ||||||||
| Accession | Primary (citable) accession number: P37332 Secondary accession number(s): Q13FT3 | ||||||||
| Entry history |
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| 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


