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Protein

Ferroxidase

Gene

bfrB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Unreviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Catalytic activityi

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi10 – 101Iron 1; via tele nitrogenCombined sources
Metal bindingi10 – 101Iron 2; via tele nitrogenCombined sources
Metal bindingi18 – 181Iron 3Combined sources
Metal bindingi51 – 511Iron 3Combined sources
Metal bindingi51 – 511Iron 4Combined sources
Metal bindingi51 – 511Iron 5Combined sources
Metal bindingi51 – 511Iron 6Combined sources
Metal bindingi52 – 521Iron (heme 1 axial ligand)Combined sources
Metal bindingi52 – 521Iron (heme 2 axial ligand)Combined sources
Metal bindingi54 – 541Iron 3; via pros nitrogenCombined sources
Metal bindingi94 – 941Iron 4Combined sources
Metal bindingi94 – 941Iron 5Combined sources
Metal bindingi94 – 941Iron 6Combined sources
Metal bindingi107 – 1071Iron 1; via pros nitrogenCombined sources
Metal bindingi107 – 1071Iron 2; via pros nitrogenCombined sources
Metal bindingi118 – 1181Iron 1Combined sources
Metal bindingi118 – 1181Iron 4Combined sources
Metal bindingi118 – 1181Iron 7Combined sources
Metal bindingi127 – 1271Iron 3Combined sources
Metal bindingi127 – 1271Iron 4Combined sources
Metal bindingi127 – 1271Iron 5Combined sources
Metal bindingi127 – 1271Iron 6Combined sources
Metal bindingi130 – 1301Iron 4; via pros nitrogenCombined sources
Metal bindingi130 – 1301Iron 5; via pros nitrogenCombined sources
Metal bindingi130 – 1301Iron 6; via pros nitrogenCombined sources
Metal bindingi153 – 1531Iron 3; via tele nitrogenCombined sources
Metal bindingi153 – 1531Iron 4; via tele nitrogenCombined sources
Metal bindingi153 – 1531Iron 5; via tele nitrogenCombined sources
Metal bindingi153 – 1531Iron 7; via tele nitrogenCombined sources
Metal bindingi155 – 1551Iron 2; via tele nitrogenCombined sources
Metal bindingi155 – 1551Iron 3; via tele nitrogenCombined sources
Metal bindingi155 – 1551Iron 5; via tele nitrogenCombined sources
Metal bindingi155 – 1551Iron 7; via tele nitrogenCombined sources

GO - Molecular functioni

GO - Biological processi

  • intracellular sequestering of iron ion Source: PseudoCAP
  • iron ion transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Iron storageUniRule annotation

Keywords - Ligandi

HemeUniRule annotationCombined sources, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
FerroxidaseUniRule annotation (EC:1.16.3.1UniRule annotation)
Gene namesi
Name:bfrBImported
Ordered Locus Names:PA3531Imported
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)Imported
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3531.

Subcellular locationi

GO - Cellular componenti

  • cell Source: GOC
Complete GO annotation...

PTM / Processingi

Proteomic databases

PaxDbiQ9HY79.

Interactioni

Protein-protein interaction databases

STRINGi208964.PA3531.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IS7X-ray2.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
3IS8X-ray2.25A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
3ISEX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
3ISFX-ray2.07A/B/C/D/E/F1-158[»]
4E6KX-ray2.00A/B/C/D/E/F1-158[»]
4TO9X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
4TOAX-ray1.95A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
4TOBX-ray1.95A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
4TOCX-ray2.25A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
4TODX-ray2.05A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
4TOEX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
4TOFX-ray1.65A/B/C/D1-158[»]
4TOGX-ray1.80A/B/C/D1-158[»]
4TOHX-ray1.80A/B/C/D1-158[»]
5D8OX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
5D8PX-ray2.35A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
5D8QX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
5D8RX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
5D8SX-ray2.55A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
5D8XX-ray1.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
5D8YX-ray2.05A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
ProteinModelPortaliQ9HY79.
SMRiQ9HY79. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HY79.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the bacterioferritin family.UniRule annotation
Contains 1 ferritin-like diiron domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108UQY. Bacteria.
COG2193. LUCA.
InParanoidiQ9HY79.
KOiK03594.
OMAiEMKHADQ.
OrthoDBiEOG6WDSKP.
PhylomeDBiQ9HY79.

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.

Q9HY79-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGDKKVIQH LNKILGNELI AINQYFLHSR MWNDWGLKRL GAHEYHESID
60 70 80 90 100
EMKHADKLIE RILFLEGLPN LQDLGKLLIG ENTQEMLQCD LNLELKATKD
110 120 130 140 150
LREAIVHCEQ VHDYVSRDLL KDILESEEEH IDYLETQLGL IQKVGLENYL

QSHMHEDD
Length:158
Mass (Da):18,553
Last modified:March 1, 2001 - v1
Checksum:i7639729EA8E5F3FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG06919.1.
PIRiA83205.
RefSeqiNP_252221.1. NC_002516.2.
WP_003092078.1. NZ_ASJY01000572.1.

Genome annotation databases

EnsemblBacteriaiAAG06919; AAG06919; PA3531.
GeneIDi879026.
KEGGipae:PA3531.
PATRICi19841675. VBIPseAer58763_3695.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG06919.1.
PIRiA83205.
RefSeqiNP_252221.1. NC_002516.2.
WP_003092078.1. NZ_ASJY01000572.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IS7X-ray2.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
3IS8X-ray2.25A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
3ISEX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
3ISFX-ray2.07A/B/C/D/E/F1-158[»]
4E6KX-ray2.00A/B/C/D/E/F1-158[»]
4TO9X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
4TOAX-ray1.95A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
4TOBX-ray1.95A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
4TOCX-ray2.25A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
4TODX-ray2.05A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
4TOEX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
4TOFX-ray1.65A/B/C/D1-158[»]
4TOGX-ray1.80A/B/C/D1-158[»]
4TOHX-ray1.80A/B/C/D1-158[»]
5D8OX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
5D8PX-ray2.35A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
5D8QX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
5D8RX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
5D8SX-ray2.55A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
5D8XX-ray1.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
5D8YX-ray2.05A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
ProteinModelPortaliQ9HY79.
SMRiQ9HY79. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA3531.

Proteomic databases

PaxDbiQ9HY79.

Protocols and materials databases

DNASUi879026.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG06919; AAG06919; PA3531.
GeneIDi879026.
KEGGipae:PA3531.
PATRICi19841675. VBIPseAer58763_3695.

Organism-specific databases

PseudoCAPiPA3531.

Phylogenomic databases

eggNOGiENOG4108UQY. Bacteria.
COG2193. LUCA.
InParanoidiQ9HY79.
KOiK03594.
OMAiEMKHADQ.
OrthoDBiEOG6WDSKP.
PhylomeDBiQ9HY79.

Miscellaneous databases

EvolutionaryTraceiQ9HY79.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228Imported.
  2. "Structural studies of bacterioferritin B from Pseudomonas aeruginosa suggest a gating mechanism for iron uptake via the ferroxidase center ."
    Weeratunga S.K., Lovell S., Yao H., Battaile K.P., Fischer C.J., Gee C.E., Rivera M.
    Biochemistry 49:1160-1175(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH HEME AND IRON.
  3. "The structure of the BfrB-Bfd complex reveals protein-protein interactions enabling iron release from bacterioferritin."
    Yao H., Wang Y., Lovell S., Kumar R., Ruvinsky A.M., Battaile K.P., Vakser I.A., Rivera M.
    J. Am. Chem. Soc. 134:13470-13481(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME.
  4. "Concerted motions networking pores and distant ferroxidase centers enable bacterioferritin function and iron traffic."
    Yao H., Rui H., Kumar R., Eshelman K., Lovell S., Battaile K.P., Im W., Rivera M.
    Biochemistry 54:1611-1627(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH HEME AND IRON.
  5. "Characterization of the Bacterioferritin/Bacterioferritin Associated Ferredoxin Protein-Protein Interaction in Solution and Determination of Binding Energy Hot Spots."
    Wang Y., Yao H., Cheng Y., Lovell S., Battaile K.P., Midaugh C.R., Rivera M.
    Biochemistry 54:6162-6175(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).

Entry informationi

Entry nameiQ9HY79_PSEAE
AccessioniPrimary (citable) accession number: Q9HY79
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: April 13, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.