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ECOLI:BFR

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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

PMID:10769510[1]

ECO:0000314

F

Fig 2

complete
CACAO 11441

part_of

GO:0016020

membrane

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:7664064[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0ABD3

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0ABD3

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

PMID:8477705[4]

ECO:0000303

author statement without traceable support used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:7032515[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0020037

heme binding

PMID:7032515[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006880

intracellular sequestering of iron ion

PMID:8477705[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005506

iron ion binding

PMID:8477705[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004322

ferroxidase activity

PMID:10769150[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006826

iron ion transport

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002024

P

Seeded From UniProt

complete

involved_in

GO:0006879

cellular iron ion homeostasis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002024
InterPro:IPR008331

P

Seeded From UniProt

complete

enables

GO:0008199

ferric iron binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002024
InterPro:IPR008331

F

Seeded From UniProt

complete

enables

GO:0004322

ferroxidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.16.3.1

F

Seeded From UniProt

complete

involved_in

GO:0006879

cellular iron ion homeostasis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0409

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Sy, M et al. (2000) Intraabdominal desmoid tumor. JBR-BTR 83 24 PubMed GONUTS page
  2. 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
  3. Frolow, F et al. (1994) Structure of a unique twofold symmetric haem-binding site. Nat. Struct. Biol. 1 453-60 PubMed GONUTS page
  4. 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. 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
  6. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  7. Yang, X et al. (2000) The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin. Biochemistry 39 4915-23 PubMed GONUTS page