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ECOLI:BFR
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | bfr | |
| Protein Name(s) | Bacterioferritin
BFR Cytochrome b-1 Cytochrome b-557 | |
| External Links | ||
| UniProt | P0ABD3 | |
| EMBL | M27176 AF058450 U18997 U00096 AP009048 L28106 | |
| PIR | JV0032 | |
| RefSeq | NP_417795.1 WP_000675504.1 | |
| PDB | 1BCF 1BFR 2HTN 2VXI 2Y3Q 3E1J 3E1L 3E1M 3E1N 3E1O 3E1P 3E1Q 3E2C 3GHQ 4CVP 4CVR 4CVS 4CVT 4U3G 4XKS 4XKT 4XKU | |
| PDBsum | 1BCF 1BFR 2HTN 2VXI 2Y3Q 3E1J 3E1L 3E1M 3E1N 3E1O 3E1P 3E1Q 3E2C 3GHQ 4CVP 4CVR 4CVS 4CVT 4U3G 4XKS 4XKT 4XKU | |
| ProteinModelPortal | P0ABD3 | |
| SMR | P0ABD3 | |
| BioGrid | 4262466 | |
| DIP | DIP-36167N | |
| IntAct | P0ABD3 | |
| STRING | 511145.b3336 | |
| EPD | P0ABD3 | |
| PaxDb | P0ABD3 | |
| PRIDE | P0ABD3 | |
| EnsemblBacteria | AAC76361 BAE77955 | |
| GeneID | 947839 | |
| KEGG | ecj:JW3298 eco:b3336 | |
| PATRIC | 32122104 | |
| EchoBASE | EB0111 | |
| EcoGene | EG10113 | |
| eggNOG | ENOG4108UQY COG2193 | |
| HOGENOM | HOG000262383 | |
| InParanoid | P0ABD3 | |
| KO | K03594 | |
| OMA | EMKHADQ | |
| OrthoDB | EOG6WDSKP | |
| PhylomeDB | P0ABD3 | |
| BioCyc | EcoCyc:EG10113-MONOMER ECOL316407:JW3298-MONOMER | |
| BRENDA | 1.16.3.1 | |
| EvolutionaryTrace | P0ABD3 | |
| PRO | PR:P0ABD3 | |
| Proteomes | UP000000318 UP000000625 | |
| GO | GO:0005829 GO:0016020 GO:0008199 GO:0004322 GO:0020037 GO:0042802 GO:0005506 GO:0016491 GO:0006880 GO:0006826 | |
| Gene3D | 1.20.1260.10 | |
| InterPro | IPR002024 IPR009040 IPR009078 IPR012347 IPR008331 | |
| Pfam | PF00210 | |
| PIRSF | PIRSF002560 | |
| PRINTS | PR00601 | |
| SUPFAM | SSF47240 | |
| TIGRFAMs | TIGR00754 | |
| PROSITE | PS00549 PS50905 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0004322 |
ferroxidase activity |
ECO:0000314 |
F |
Fig 2 |
complete | |||||
|
part_of |
GO:0016020 |
membrane |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000303 |
author statement without traceable support used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0020037 |
heme binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006880 |
intracellular sequestering of iron ion |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005506 |
iron ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004322 |
ferroxidase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006826 |
iron ion transport |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006879 |
cellular iron ion homeostasis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008199 |
ferric iron binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004322 |
ferroxidase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006879 |
cellular iron ion homeostasis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Sy, M et al. (2000) Intraabdominal desmoid tumor. JBR-BTR 83 24 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
- ↑ Frolow, F et al. (1994) Structure of a unique twofold symmetric haem-binding site. Nat. Struct. Biol. 1 453-60 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 Andrews, SC et al. (1993) Overproduction, purification and characterization of the bacterioferritin of Escherichia coli and a C-terminally extended variant. Eur. J. Biochem. 213 329-38 PubMed GONUTS page
- ↑ 5.0 5.1 Yariv, J et al. (1981) The composition and the structure of bacterioferritin of Escherichia coli. Biochem. J. 197 171-5 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
- ↑ Yang, X et al. (2000) The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin. Biochemistry 39 4915-23 PubMed GONUTS page
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