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P0ABD3

- BFR_ECOLI

UniProt

P0ABD3 - BFR_ECOLI

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Protein

Bacterioferritin

Gene
bfr, b3336, JW3298
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Iron-storage protein, whose ferroxidase center binds Fe2+ ions, oxidizes them by dioxygen to Fe3+, and participates in the subsequent Fe3+ oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.2 Publications

Catalytic activityi

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.3 Publications

Cofactori

Binds 1 heme B (iron-protoporphyrin IX) group per dimer.2 Publications
Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center. In BFR, the ferroxidase center appears to function as a true di-iron catalytic cofactor, rather than as a pore for the transfer of iron into the central cavity, as found for eukaryotic ferritins.1 Publication

Enzyme regulationi

Iron oxidation is inhibited by Zn2+, which binds at the ferroxidase center with a higher affinity that Fe2+. The occupation of the ferroxidase center by Zn2+ also severely restricts the ability of BFR to form an iron core.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181Iron 1
Metal bindingi46 – 461Iron 3
Metal bindingi50 – 501Iron 3
Metal bindingi51 – 511Iron 1
Metal bindingi51 – 511Iron 2
Metal bindingi52 – 521Iron (heme axial ligand); shared with dimeric partner
Metal bindingi54 – 541Iron 1
Metal bindingi94 – 941Iron 2
Metal bindingi127 – 1271Iron 1
Metal bindingi127 – 1271Iron 2
Metal bindingi130 – 1301Iron 2

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. ferroxidase activity Source: UniProtKB-EC
  3. heme binding Source: EcoCyc
  4. identical protein binding Source: EcoCyc
  5. iron ion binding Source: EcoCyc
  6. oxidoreductase activity Source: EcoliWiki

GO - Biological processi

  1. intracellular sequestering of iron ion Source: EcoCyc
  2. iron ion transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10113-MONOMER.
ECOL316407:JW3298-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Bacterioferritin (EC:1.16.3.1)
Short name:
BFR
Alternative name(s):
Cytochrome b-1
Cytochrome b-557
Gene namesi
Name:bfr
Ordered Locus Names:b3336, JW3298
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10113. bfr.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181E → A: Highly decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. 1 Publication
Mutagenesisi31 – 311M → H or L: No loss of heme binding. 1 Publication
Mutagenesisi46 – 461H → A: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired. 1 Publication
Mutagenesisi50 – 501D → A: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired. 1 Publication
Mutagenesisi52 – 521M → H or L: Loss of heme binding. Is still capable of accumulating iron. 1 Publication
Mutagenesisi86 – 861M → L: No loss of heme binding. 1 Publication
Mutagenesisi127 – 1271E → Q: Decreased Fe(2+) oxidation activity. Is also affected in its ability to lay down an iron core. 1 Publication
Mutagenesisi130 – 1301H → E: Decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158BacterioferritinPRO_0000192592Add
BLAST

Proteomic databases

PaxDbiP0ABD3.
PRIDEiP0ABD3.

Expressioni

Gene expression databases

GenevestigatoriP0ABD3.

Interactioni

Subunit structurei

Homooligomer of 24 subunits, arranged as 12 dimers, that are packed together to form an approximately spherical molecule with a central cavity, in which large amounts of iron can be deposited as a ferric-oxy-hydroxide mineral core.1 Publication

Protein-protein interaction databases

DIPiDIP-36167N.
IntActiP0ABD3. 2 interactions.
STRINGi511145.b3336.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 3430
Helixi38 – 6427
Helixi83 – 11028
Helixi114 – 14431
Helixi146 – 1516

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCFX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
1BFRX-ray2.94A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
2HTNX-ray2.50A/B/C/D/E/F/G/H1-158[»]
2VXIX-ray1.91A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
2Y3QX-ray1.55A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1JX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1LX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1MX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1NX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1OX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1PX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E1QX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
3E2CX-ray1.80A/B1-158[»]
3GHQX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
ProteinModelPortaliP0ABD3.
SMRiP0ABD3. Positions 1-157.

Miscellaneous databases

EvolutionaryTraceiP0ABD3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 145145Ferritin-like diironAdd
BLAST

Sequence similaritiesi

Belongs to the bacterioferritin family.

Phylogenomic databases

eggNOGiCOG2193.
HOGENOMiHOG000262383.
KOiK03594.
OMAiCTRNTAV.
OrthoDBiEOG6WDSKP.
PhylomeDBiP0ABD3.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PfamiPF00210. Ferritin. 1 hit.
[Graphical view]
PIRSFiPIRSF002560. Bacterioferritin. 1 hit.
PRINTSiPR00601. BACFERRITIN.
SUPFAMiSSF47240. SSF47240. 1 hit.
TIGRFAMsiTIGR00754. bfr. 1 hit.
PROSITEiPS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABD3-1 [UniParc]FASTAAdd to Basket

« Hide

MKGDTKVINY LNKLLGNELV AINQYFLHAR MFKNWGLKRL NDVEYHESID    50
EMKHADRYIE RILFLEGLPN LQDLGKLNIG EDVEEMLRSD LALELDGAKN 100
LREAIGYADS VHDYVSRDMM IEILRDEEGH IDWLETELDL IQKMGLQNYL 150
QAQIREEG 158
Length:158
Mass (Da):18,495
Last modified:October 25, 2005 - v1
Checksum:iA6C86CE1CD8F865A
GO

Mass spectrometryi

Molecular mass is 18496±2 Da from positions 1 - 158. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 73TKV → VKI in strain: ECOR 30.
Natural varianti38 – 381K → M in strain: ECOR 30.
Natural varianti57 – 571R → K in strain: ECOR 30.
Natural varianti68 – 681L → I in strain: ECOR 30.
Natural varianti78 – 781N → G in strain: ECOR 30.
Natural varianti88 – 881R → Q in strain: ECOR 30.
Natural varianti92 – 921A → R in strain: ECOR 30.
Natural varianti96 – 961D → E in strain: ECOR 30.
Natural varianti100 – 1001N → D in strain: ECOR 30.
Natural varianti106 – 1061G → A in strain: ECOR 30.
Natural varianti125 – 1251R → A in strain: ECOR 30.
Natural varianti142 – 1443QKM → GKI in strain: ECOR 30.
Natural varianti152 – 1587AQIREEG → SQIKVKD in strain: ECOR 30.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531K → M AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M27176 mRNA. Translation: AAC13987.1.
AF058450 Genomic DNA. Translation: AAC14288.1.
U18997 Genomic DNA. Translation: AAA58133.1.
U00096 Genomic DNA. Translation: AAC76361.1.
AP009048 Genomic DNA. Translation: BAE77955.1.
L28106 Genomic DNA. Translation: AAC36929.1.
PIRiJV0032. FREC.
RefSeqiNP_417795.1. NC_000913.3.
YP_492096.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76361; AAC76361; b3336.
BAE77955; BAE77955; BAE77955.
GeneIDi12933472.
947839.
KEGGiecj:Y75_p3840.
eco:b3336.
PATRICi32122104. VBIEscCol129921_3429.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M27176 mRNA. Translation: AAC13987.1 .
AF058450 Genomic DNA. Translation: AAC14288.1 .
U18997 Genomic DNA. Translation: AAA58133.1 .
U00096 Genomic DNA. Translation: AAC76361.1 .
AP009048 Genomic DNA. Translation: BAE77955.1 .
L28106 Genomic DNA. Translation: AAC36929.1 .
PIRi JV0032. FREC.
RefSeqi NP_417795.1. NC_000913.3.
YP_492096.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BCF X-ray 2.90 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
1BFR X-ray 2.94 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1-158 [» ]
2HTN X-ray 2.50 A/B/C/D/E/F/G/H 1-158 [» ]
2VXI X-ray 1.91 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
2Y3Q X-ray 1.55 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
3E1J X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
3E1L X-ray 2.50 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
3E1M X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
3E1N X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
3E1O X-ray 2.95 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
3E1P X-ray 2.40 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
3E1Q X-ray 2.60 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
3E2C X-ray 1.80 A/B 1-158 [» ]
3GHQ X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
ProteinModelPortali P0ABD3.
SMRi P0ABD3. Positions 1-157.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-36167N.
IntActi P0ABD3. 2 interactions.
STRINGi 511145.b3336.

Proteomic databases

PaxDbi P0ABD3.
PRIDEi P0ABD3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76361 ; AAC76361 ; b3336 .
BAE77955 ; BAE77955 ; BAE77955 .
GeneIDi 12933472.
947839.
KEGGi ecj:Y75_p3840.
eco:b3336.
PATRICi 32122104. VBIEscCol129921_3429.

Organism-specific databases

EchoBASEi EB0111.
EcoGenei EG10113. bfr.

Phylogenomic databases

eggNOGi COG2193.
HOGENOMi HOG000262383.
KOi K03594.
OMAi CTRNTAV.
OrthoDBi EOG6WDSKP.
PhylomeDBi P0ABD3.

Enzyme and pathway databases

BioCyci EcoCyc:EG10113-MONOMER.
ECOL316407:JW3298-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0ABD3.
PROi P0ABD3.

Gene expression databases

Genevestigatori P0ABD3.

Family and domain databases

Gene3Di 1.20.1260.10. 1 hit.
InterProi IPR002024. Bacterioferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR008331. Ferritin_DPS_dom.
[Graphical view ]
Pfami PF00210. Ferritin. 1 hit.
[Graphical view ]
PIRSFi PIRSF002560. Bacterioferritin. 1 hit.
PRINTSi PR00601. BACFERRITIN.
SUPFAMi SSF47240. SSF47240. 1 hit.
TIGRFAMsi TIGR00754. bfr. 1 hit.
PROSITEi PS00549. BACTERIOFERRITIN. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of Escherichia coli K-12."
    Andrews S.C., Harrison P.M., Guest J.R.
    J. Bacteriol. 171:3940-3947(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Noorani S.M., Lindahl L., Zengel J.M.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ECOR 30.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Amino acid sequence of the bacterioferritin (cytochrome b1) of Escherichia coli-K12."
    Andrews S.C., Smith J.M.A., Guest J.R., Harrison P.M.
    Biochem. Biophys. Res. Commun. 158:489-496(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-87.
    Strain: K12.
  6. "Escherichia coli contains a set of genes homologous to those involved in protein secretion, DNA uptake and the assembly of type-4 fimbriae in other bacteria."
    Whitchurch C.B., Mattick J.S.
    Gene 150:9-15(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-158.
    Strain: K12.
  7. "Site-directed replacement of the coaxial heme ligands of bacterioferritin generates heme-free variants."
    Andrews S.C., Le Brun N.E., Barynin V., Thomson A.J., Moore G.R., Guest J.R., Harrison P.M.
    J. Biol. Chem. 270:23268-23274(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: HEME-BINDING, MASS SPECTROMETRY, MUTAGENESIS OF MET-31; MET-52 AND MET-86.
    Strain: K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin."
    Yang X., Le Brun N.E., Thomson A.J., Moore G.R., Chasteen N.D.
    Biochemistry 39:4915-4923(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
  10. "Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center."
    Baaghil S., Lewin A., Moore G.R., Le Brun N.E.
    Biochemistry 42:14047-14056(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ROLE OF THE FERROXIDASE CENTER IN CORE FORMATION, CATALYTIC ACTIVITY, ENZYME REGULATION, MUTAGENESIS OF GLU-18; GLU-127 AND HIS-130.
  11. "Structure of a unique twofold symmetric haem-binding site."
    Frolow F., Kalb A.J., Yariv J.
    Nat. Struct. Biol. 1:453-460(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH HEME AND MANGANESE IONS.
  12. "Structure of a monoclinic crystal form of cyctochrome b1 (bacterioferritin) from E. coli."
    Dautant A., Meyer J.-B., Yariv J., Precigoux G., Sweet R.M., Kalb A.J., Frolow F.
    Acta Crystallogr. D 54:16-24(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) IN COMPLEX WITH HEME AND MANGANESE IONS, SUBUNIT.
  13. "Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form."
    van Eerde A., Wolterink-van Loo S., van der Oost J., Dijkstra B.W.
    Acta Crystallogr. F 62:1061-1066(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH HEME; IRON AND ZINC IONS.
    Strain: B / BL21.
  14. "Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy."
    Lawson T.L., Crow A., Lewin A., Yasmin S., Moore G.R., Le Brun N.E.
    Biochemistry 48:9031-9039(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANTS PHE-35 AND PHE-133 IN COMPLEX WITH HEME AND IRON IONS, CATALYTIC ACTIVITY, ENZYME REGULATION.
    Strain: K12 / JM109 / ATCC 53323.
  15. "Structural basis for iron mineralization by bacterioferritin."
    Crow A., Lawson T.L., Lewin A., Moore G.R., Le Brun N.E.
    J. Am. Chem. Soc. 131:6808-6813(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF METAL-FREE APOPROTEIN AND IN COMPLEXES WITH ZN(2+); FE(2+); FE(3+) AND HEME, COFACTOR, INTERNAL SURFACE IRON-BINDING SITE, MUTAGENESIS OF HIS-46 AND ASP-50, MECHANISM OF IRON MINERALIZATION.
    Strain: K12 / JM109 / ATCC 53323.
  16. "Structural and mechanistic studies of a stabilized subunit dimer variant of Escherichia coli bacterioferritin identify residues required for core formation."
    Wong S.G., Tom-Yew S.A., Lewin A., Le Brun N.E., Moore G.R., Murphy M.E., Mauk A.G.
    J. Biol. Chem. 284:18873-18881(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ARG-128/ARG-135 DIMER IN COMPLEX WITH HEME AND ZINC IONS.
  17. "The binding of haem and zinc in the 1.9 A X-ray structure of Escherichia coli bacterioferritin."
    Willies S.C., Isupov M.N., Garman E.F., Littlechild J.A.
    J. Biol. Inorg. Chem. 14:201-207(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH HEME AND ZINC IONS.
    Strain: B / BL21.
  18. "Monitoring and validating active site redox states in protein crystals."
    Antonyuk S.V., Hough M.A.
    Biochim. Biophys. Acta 1814:778-784(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH HEME.

Entry informationi

Entry nameiBFR_ECOLI
AccessioniPrimary (citable) accession number: P0ABD3
Secondary accession number(s): O68931, P11056, Q2M701
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: May 14, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The internal surface iron site that binds iron 3 is important for the mineralization phase but not for Fe2+ binding and oxidation at the ferroxidase center.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi