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Bacterioferritin (BFR) (EC 1.16.3.1) (Cytochrome b-1) (Cytochrome b-557)

 BFR_ECOLI               Reviewed;         158 AA.
P0ABD3; O68931; P11056; Q2M701;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 1.
08-MAY-2019, entry version 110.
RecName: Full=Bacterioferritin;
Short=BFR;
EC=1.16.3.1;
AltName: Full=Cytochrome b-1;
AltName: Full=Cytochrome b-557;
Name=bfr; OrderedLocusNames=b3336, JW3298;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=2661540; DOI=10.1128/jb.171.7.3940-3947.1989;
Andrews S.C., Harrison P.M., Guest J.R.;
"Cloning, sequencing, and mapping of the bacterioferritin gene (bfr)
of Escherichia coli K-12.";
J. Bacteriol. 171:3940-3947(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ECOR 30;
Noorani S.M., Lindahl L., Zengel J.M.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 1-87.
STRAIN=K12;
PubMed=2644932; DOI=10.1016/S0006-291X(89)80075-0;
Andrews S.C., Smith J.M.A., Guest J.R., Harrison P.M.;
"Amino acid sequence of the bacterioferritin (cytochrome b1) of
Escherichia coli-K12.";
Biochem. Biophys. Res. Commun. 158:489-496(1989).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-158.
STRAIN=K12;
PubMed=7959070; DOI=10.1016/0378-1119(94)90851-6;
Whitchurch C.B., Mattick J.S.;
"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.";
Gene 150:9-15(1994).
[7]
HEME-BINDING, MASS SPECTROMETRY, AND MUTAGENESIS OF MET-31; MET-52 AND
MET-86.
STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
PubMed=7559480; DOI=10.1074/jbc.270.40.23268;
Andrews S.C., Le Brun N.E., Barynin V., Thomson A.J., Moore G.R.,
Guest J.R., Harrison P.M.;
"Site-directed replacement of the coaxial heme ligands of
bacterioferritin generates heme-free variants.";
J. Biol. Chem. 270:23268-23274(1995).
[8]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
PubMed=10769150; DOI=10.1021/bi992631f;
Yang X., Le Brun N.E., Thomson A.J., Moore G.R., Chasteen N.D.;
"The iron oxidation and hydrolysis chemistry of Escherichia coli
bacterioferritin.";
Biochemistry 39:4915-4923(2000).
[10]
FUNCTION, ROLE OF THE FERROXIDASE CENTER IN CORE FORMATION, CATALYTIC
ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF GLU-18; GLU-127 AND
HIS-130.
PubMed=14636073; DOI=10.1021/bi035253u;
Baaghil S., Lewin A., Moore G.R., Le Brun N.E.;
"Core formation in Escherichia coli bacterioferritin requires a
functional ferroxidase center.";
Biochemistry 42:14047-14056(2003).
[11]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH HEME AND
MANGANESE IONS.
PubMed=7664064; DOI=10.1038/nsb0794-453;
Frolow F., Kalb A.J., Yariv J.;
"Structure of a unique twofold symmetric haem-binding site.";
Nat. Struct. Biol. 1:453-460(1994).
[12]
X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) IN COMPLEX WITH HEME AND
MANGANESE IONS, AND SUBUNIT.
PubMed=9867433; DOI=10.1107/S0907444997006811;
Dautant A., Meyer J.-B., Yariv J., Precigoux G., Sweet R.M.,
Kalb A.J., Frolow F.;
"Structure of a monoclinic crystal form of cyctochrome b1
(bacterioferritin) from E. coli.";
Acta Crystallogr. D 54:16-24(1998).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH HEME; IRON AND
ZINC IONS.
STRAIN=B / BL21;
PubMed=17077480; DOI=10.1107/S1744309106039583;
van Eerde A., Wolterink-van Loo S., van der Oost J., Dijkstra B.W.;
"Fortuitous structure determination of 'as-isolated' Escherichia coli
bacterioferritin in a novel crystal form.";
Acta Crystallogr. F 62:1061-1066(2006).
[14]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANTS PHE-35 AND PHE-133 IN
COMPLEX WITH HEME AND IRON IONS, CATALYTIC ACTIVITY, AND ACTIVITY
REGULATION.
STRAIN=K12 / JM109 / ATCC 53323;
PubMed=19705876; DOI=10.1021/bi900869x;
Lawson T.L., Crow A., Lewin A., Yasmin S., Moore G.R., Le Brun N.E.;
"Monitoring the iron status of the ferroxidase center of Escherichia
coli bacterioferritin using fluorescence spectroscopy.";
Biochemistry 48:9031-9039(2009).
[15]
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, AND
MECHANISM OF IRON MINERALIZATION.
STRAIN=K12 / JM109 / ATCC 53323;
PubMed=19391621; DOI=10.1021/ja8093444;
Crow A., Lawson T.L., Lewin A., Moore G.R., Le Brun N.E.;
"Structural basis for iron mineralization by bacterioferritin.";
J. Am. Chem. Soc. 131:6808-6813(2009).
[16]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ARG-128/ARG-135 DIMER
IN COMPLEX WITH HEME AND ZINC IONS.
PubMed=19439409; DOI=10.1074/jbc.M901747200;
Wong S.G., Tom-Yew S.A., Lewin A., Le Brun N.E., Moore G.R.,
Murphy M.E., Mauk A.G.;
"Structural and mechanistic studies of a stabilized subunit dimer
variant of Escherichia coli bacterioferritin identify residues
required for core formation.";
J. Biol. Chem. 284:18873-18881(2009).
[17]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH HEME AND ZINC
IONS.
STRAIN=B / BL21;
PubMed=18946693; DOI=10.1007/s00775-008-0438-8;
Willies S.C., Isupov M.N., Garman E.F., Littlechild J.A.;
"The binding of haem and zinc in the 1.9 A X-ray structure of
Escherichia coli bacterioferritin.";
J. Biol. Inorg. Chem. 14:201-207(2009).
[18]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH HEME.
PubMed=21215826; DOI=10.1016/j.bbapap.2010.12.017;
Antonyuk S.V., Hough M.A.;
"Monitoring and validating active site redox states in protein
crystals.";
Biochim. Biophys. Acta 1814:778-784(2011).
-!- FUNCTION: Iron-storage protein, whose ferroxidase center binds
Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates
in the subsequent Fe(3+) 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.
{ECO:0000269|PubMed:10769150, ECO:0000269|PubMed:14636073}.
-!- CATALYTIC ACTIVITY:
Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
EC=1.16.3.1; Evidence={ECO:0000269|PubMed:10769150,
ECO:0000269|PubMed:14636073, ECO:0000269|PubMed:19705876};
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:19391621};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
{ECO:0000269|PubMed:19391621};
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000269|PubMed:19391621};
Note=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. {ECO:0000269|PubMed:19391621};
-!- ACTIVITY REGULATION: Iron oxidation is inhibited by Zn(2+), which
binds at the ferroxidase center with a higher affinity that
Fe(2+). The occupation of the ferroxidase center by Zn(2+) also
severely restricts the ability of BFR to form an iron core.
{ECO:0000269|PubMed:10769150, ECO:0000269|PubMed:14636073,
ECO:0000269|PubMed:19705876}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:17077480, ECO:0000269|PubMed:18946693,
ECO:0000269|PubMed:19439409, ECO:0000269|PubMed:19705876,
ECO:0000269|PubMed:21215826, ECO:0000269|PubMed:7664064,
ECO:0000269|PubMed:9867433}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-907496, EBI-907496;
-!- MASS SPECTROMETRY: Mass=18496; Mass_error=2; Method=Electrospray;
Range=1-158; Evidence={ECO:0000269|PubMed:7559480};
-!- MISCELLANEOUS: The internal surface iron site that binds iron 3 is
important for the mineralization phase but not for Fe(2+) binding
and oxidation at the ferroxidase center.
-!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}.
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EMBL; M27176; AAC13987.1; -; mRNA.
EMBL; AF058450; AAC14288.1; -; Genomic_DNA.
EMBL; U18997; AAA58133.1; -; Genomic_DNA.
EMBL; U00096; AAC76361.1; -; Genomic_DNA.
EMBL; AP009048; BAE77955.1; -; Genomic_DNA.
EMBL; L28106; AAC36929.1; -; Genomic_DNA.
PIR; JV0032; FREC.
RefSeq; NP_417795.1; NC_000913.3.
RefSeq; WP_000675504.1; NZ_LN832404.1.
PDB; 1BCF; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 1BFR; X-ray; 2.94 A; 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.
PDB; 2HTN; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-158.
PDB; 2VXI; X-ray; 1.91 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 2Y3Q; X-ray; 1.55 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1J; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1L; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1M; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1N; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1O; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1P; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1Q; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E2C; X-ray; 1.80 A; A/B=1-158.
PDB; 3GHQ; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 4CVP; X-ray; 2.11 A; A=1-158.
PDB; 4CVR; X-ray; 1.10 A; A=1-158.
PDB; 4CVS; X-ray; 1.39 A; A=1-158.
PDB; 4CVT; X-ray; 1.79 A; A=1-158.
PDB; 4U3G; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 4XKS; X-ray; 1.57 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 4XKT; X-ray; 1.82 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 4XKU; X-ray; 1.78 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 5XGO; X-ray; 1.99 A; A/B/C/D/E/F/G/H/I/J/K/L=138-158.
PDBsum; 1BCF; -.
PDBsum; 1BFR; -.
PDBsum; 2HTN; -.
PDBsum; 2VXI; -.
PDBsum; 2Y3Q; -.
PDBsum; 3E1J; -.
PDBsum; 3E1L; -.
PDBsum; 3E1M; -.
PDBsum; 3E1N; -.
PDBsum; 3E1O; -.
PDBsum; 3E1P; -.
PDBsum; 3E1Q; -.
PDBsum; 3E2C; -.
PDBsum; 3GHQ; -.
PDBsum; 4CVP; -.
PDBsum; 4CVR; -.
PDBsum; 4CVS; -.
PDBsum; 4CVT; -.
PDBsum; 4U3G; -.
PDBsum; 4XKS; -.
PDBsum; 4XKT; -.
PDBsum; 4XKU; -.
PDBsum; 5XGO; -.
SMR; P0ABD3; -.
BioGrid; 4262466; 23.
DIP; DIP-36167N; -.
IntAct; P0ABD3; 3.
STRING; 511145.b3336; -.
EPD; P0ABD3; -.
jPOST; P0ABD3; -.
PaxDb; P0ABD3; -.
PRIDE; P0ABD3; -.
EnsemblBacteria; AAC76361; AAC76361; b3336.
EnsemblBacteria; BAE77955; BAE77955; BAE77955.
GeneID; 947839; -.
KEGG; ecj:JW3298; -.
KEGG; eco:b3336; -.
PATRIC; fig|1411691.4.peg.3395; -.
EchoBASE; EB0111; -.
EcoGene; EG10113; bfr.
eggNOG; ENOG4108UQY; Bacteria.
eggNOG; COG2193; LUCA.
HOGENOM; HOG000262383; -.
InParanoid; P0ABD3; -.
KO; K03594; -.
PhylomeDB; P0ABD3; -.
BioCyc; EcoCyc:EG10113-MONOMER; -.
BioCyc; ECOL316407:JW3298-MONOMER; -.
BioCyc; MetaCyc:EG10113-MONOMER; -.
BRENDA; 1.16.3.1; 2026.
EvolutionaryTrace; P0ABD3; -.
PRO; PR:P0ABD3; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
GO; GO:0004322; F:ferroxidase activity; IDA:EcoCyc.
GO; GO:0020037; F:heme binding; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
GO; GO:0016491; F:oxidoreductase activity; NAS:EcoliWiki.
GO; GO:0006880; P:intracellular sequestering of iron ion; IDA:EcoCyc.
GO; GO:0006826; P:iron ion transport; IEA:InterPro.
CDD; cd00907; Bacterioferritin; 1.
Gene3D; 1.20.1260.10; -; 1.
InterPro; IPR002024; Bacterioferritin.
InterPro; IPR012347; Ferritin-like.
InterPro; IPR009040; Ferritin-like_diiron.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR008331; Ferritin_DPS_dom.
Pfam; PF00210; Ferritin; 1.
PIRSF; PIRSF002560; Bacterioferritin; 1.
PRINTS; PR00601; BACFERRITIN.
SUPFAM; SSF47240; SSF47240; 1.
TIGRFAMs; TIGR00754; bfr; 1.
PROSITE; PS00549; BACTERIOFERRITIN; 1.
PROSITE; PS50905; FERRITIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Heme;
Iron; Iron storage; Metal-binding; Oxidoreductase; Reference proteome.
CHAIN 1 158 Bacterioferritin.
/FTId=PRO_0000192592.
DOMAIN 1 145 Ferritin-like diiron.
{ECO:0000255|PROSITE-ProRule:PRU00085}.
METAL 18 18 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 46 46 Iron 3. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 50 50 Iron 3. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 51 51 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 51 51 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 52 52 Iron (heme axial ligand); shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 54 54 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 94 94 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 127 127 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 127 127 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 130 130 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
VARIANT 5 7 TKV -> VKI (in strain: ECOR 30).
VARIANT 38 38 K -> M (in strain: ECOR 30).
VARIANT 57 57 R -> K (in strain: ECOR 30).
VARIANT 68 68 L -> I (in strain: ECOR 30).
VARIANT 78 78 N -> G (in strain: ECOR 30).
VARIANT 88 88 R -> Q (in strain: ECOR 30).
VARIANT 92 92 A -> R (in strain: ECOR 30).
VARIANT 96 96 D -> E (in strain: ECOR 30).
VARIANT 100 100 N -> D (in strain: ECOR 30).
VARIANT 106 106 G -> A (in strain: ECOR 30).
VARIANT 125 125 R -> A (in strain: ECOR 30).
VARIANT 142 144 QKM -> GKI (in strain: ECOR 30).
VARIANT 152 158 AQIREEG -> SQIKVKD (in strain: ECOR 30).
MUTAGEN 18 18 E->A: Highly decreased Fe(2+) oxidation
activity. Is also severely restricted in
its ability to lay down an iron core.
{ECO:0000269|PubMed:14636073}.
MUTAGEN 31 31 M->H,L: No loss of heme binding.
{ECO:0000269|PubMed:7559480}.
MUTAGEN 46 46 H->A: Fe(2+)-binding and single turnover
oxidation at the ferroxidase center occur
normally but iron mineralization within
the cavity is significantly impaired.
{ECO:0000269|PubMed:19391621}.
MUTAGEN 50 50 D->A: Fe(2+)-binding and single turnover
oxidation at the ferroxidase center occur
normally but iron mineralization within
the cavity is significantly impaired.
{ECO:0000269|PubMed:19391621}.
MUTAGEN 52 52 M->H,L: Loss of heme binding. Is still
capable of accumulating iron.
{ECO:0000269|PubMed:7559480}.
MUTAGEN 86 86 M->L: No loss of heme binding.
{ECO:0000269|PubMed:7559480}.
MUTAGEN 127 127 E->Q: Decreased Fe(2+) oxidation
activity. Is also affected in its ability
to lay down an iron core.
{ECO:0000269|PubMed:14636073}.
MUTAGEN 130 130 H->E: Decreased Fe(2+) oxidation
activity. Is also severely restricted in
its ability to lay down an iron core.
{ECO:0000269|PubMed:14636073}.
CONFLICT 53 53 K -> M (in Ref. 5; AA sequence).
{ECO:0000305}.
HELIX 5 34 {ECO:0000244|PDB:4CVR}.
HELIX 38 64 {ECO:0000244|PDB:4CVR}.
HELIX 83 110 {ECO:0000244|PDB:4CVR}.
HELIX 114 144 {ECO:0000244|PDB:4CVR}.
HELIX 146 152 {ECO:0000244|PDB:4CVR}.
SEQUENCE 158 AA; 18495 MW; A6C86CE1CD8F865A CRC64;
MKGDTKVINY LNKLLGNELV AINQYFLHAR MFKNWGLKRL NDVEYHESID EMKHADRYIE
RILFLEGLPN LQDLGKLNIG EDVEEMLRSD LALELDGAKN LREAIGYADS VHDYVSRDMM
IEILRDEEGH IDWLETELDL IQKMGLQNYL QAQIREEG


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EIAAB10220 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Homo sapiens,Human,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,
E1557h ELISA kit 21-OHase,CYP21,CYP21A2,CYP21B,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Cytochrome P450-C21B,Homo sapiens,Human,Steroid 21-hydroxylase 96T
U1557h CLIA 21-OHase,CYP21,CYP21A2,CYP21B,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Cytochrome P450-C21B,Homo sapiens,Human,Steroid 21-hydroxylase 96T
E1557h ELISA 21-OHase,CYP21,CYP21A2,CYP21B,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Cytochrome P450-C21B,Homo sapiens,Human,Steroid 21-hydroxylase 96T
EIAAB10224 Cyba,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,Rat,Rattus norvegic
EIAAB10222 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,Pig,Superoxide-gene
EIAAB10221 Bos taurus,Bovine,CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,S
EIAAB10219 Cyba,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Mouse,Mus musculus,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,
EIAAB10223 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,Oryctolagus cuniculus,p22 phagocyte B-cytochrome,p22phox,p22-ph
EIAAB08923 Cyp2c12,Cyp2c-12,Cyp2c40,CYPIIC12,Cytochrome P450 15-beta,Cytochrome P450 2C12, female-specific,Cytochrome P450I,Cytochrome P450-UT-1,Cytochrome P450-UT-I,Rat,Rattus norvegicus
EIAAB08901 Cyp2b1,Cyp2b-1,CYPIIB1,Cytochrome P450 2B1,Cytochrome P450b,Cytochrome P450-B,Cytochrome P450-LM2,Cytochrome P450-PB1,Cytochrome P450-PB2,Rat,Rattus norvegicus
EIAAB08920 CYP2C8,CYPIIC8,Cytochrome P450 2C8,Cytochrome P450 form 1,Cytochrome P450 IIC2,Cytochrome P450 MP-12,Cytochrome P450 MP-20,Homo sapiens,Human,S-mephenytoin 4-hydroxylase
EIAAB08851 Cyp1a2,Cyp1a-2,CYPIA2,Cytochrome P-448,Cytochrome P450 1A2,Cytochrome P-450d,Cytochrome P450-D,Rat,Rattus norvegicus
EIAAB08879 CYP26A2,CYP26B1,Cytochrome P450 26A2,Cytochrome P450 26B1,Cytochrome P450 retinoic acid-inactivating 2,Cytochrome P450RAI-2,Homo sapiens,Human,P450RAI2,Retinoic acid-metabolizing cytochrome
EIAAB08922 Cyp2c,Cyp2c11,Cyp2c-11,CYPIIC11,Cytochrome P450 2C11,Cytochrome P-450(M-1),Cytochrome P450H,Cytochrome P450-UT-2,Cytochrome P450-UT-A,Rat,Rattus norvegicus
EIAAB08974 Albendazole monooxygenase,Albendazole sulfoxidase,CYP3A3,CYP3A4,CYPIIIA3,CYPIIIA4,Cytochrome P450 3A3,Cytochrome P450 3A4,Cytochrome P450 HLp,Cytochrome P450 NF-25,Cytochrome P450-PCN1,Homo sapiens,Hu
U1557m CLIA 21-OHase,Cyp21,Cyp21a1,Cyp21a-1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Mouse,Mus musculus,Steroid 21-hydroxylase 96T
E1557m ELISA 21-OHase,Cyp21,Cyp21a1,Cyp21a-1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Mouse,Mus musculus,Steroid 21-hydroxylase 96T
E1557m ELISA kit 21-OHase,Cyp21,Cyp21a1,Cyp21a-1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Mouse,Mus musculus,Steroid 21-hydroxylase 96T
U1557p CLIA 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 96T
E1557r ELISA 21-OHase,Cyp21,Cyp21a1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Rat,Rattus norvegicus,Steroid 21-hydroxylase 96T
U1557r CLIA 21-OHase,Cyp21,Cyp21a1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Rat,Rattus norvegicus,Steroid 21-hydroxylase 96T
E1557p ELISA 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 96T
E1557b ELISA 21-OHase,Bos taurus,Bovine,CYP21,CYP21A1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Steroid 21-hydroxylase 96T
E1557p ELISA kit 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 96T
Pathways :
WP1274: cytochrome P450
WP2316: PPAR signaling pathway
WP677: Momilactone biosynthesis
WP1219: cytochrome P450
WP1502: Mitochondrial biogenesis
WP43: cytochrome P450
WP958: cytochrome P450
WP1194: cytochrome P450
WP1390: cytochrome P450
WP2430: Quercetin metabolism
WP696: Benzo(a)pyrene metabolism
WP1077: cytochrome P450

Related Genes :
[cox-1 coi cox1 NCM025 NCU16016] Cytochrome c oxidase subunit 1 (EC 1.9.3.1) (Cytochrome c oxidase polypeptide I)
[MT-CYB COB CYTB MTCYB] Cytochrome b (Complex III subunit 3) (Complex III subunit III) (Cytochrome b-c1 complex subunit 3) (Ubiquinol-cytochrome-c reductase complex cytochrome b subunit)
[CYP79F1 BUS1 SPS1 At1g16410 F3O9.21] Dihomomethionine N-hydroxylase (EC 1.14.14.42) (Cytochrome P450 79F1) (Protein BUSHY 1) (Protein SUPERSHOOT 1) (Trihomomethionine N-hydroxylase)
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMT91_24760 C4J69_22715 C7B08_25495 CR538_10415 D2F89_25795 D3Y67_22910 D9G42_11130 D9I97_22010 D9J11_25195 DP258_02540 EC3234A_36c00010 EC382_21100 ECTO6_01955 EFV06_13085 EFV16_12340 NCTC8500_02249 NCTC9037_02122 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[pep NCU02549] Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (Ubiquinol-cytochrome-c reductase complex core protein I)
[cypB cyp102A3 yrhJ BSU27160] Bifunctional cytochrome P450/NADPH--P450 reductase 2 (CYP102A3) (Fatty acid hydroxylase CypB) (Flavocytochrome P450 102A3) [Includes: Cytochrome P450 102A3 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]
[cyt-1 NCU09816] Cytochrome c1, heme protein, mitochondrial (Complex III subunit 4) (Complex III subunit IV) (Cytochrome b-c1 complex subunit 4) (Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit) (Cytochrome c-1)
[Cyp6g1 CYP6-like DDT-R Rst(2)DDT CG8453] Cytochrome P450 6g1 (EC 1.14.-.-) (CYPVIG1) (Cyp6-like protein)
[hchA A8M42_01610 AM465_15370 AWF23_018680 AWF59_019055 AZZ83_004235 B9N33_26475 BFD68_20845 C1I57_21890 C7B02_06890 CCZ14_26645 CCZ17_22700 CRT43_11430 CT143_08220 D3C88_02905 D6X47_12880 D9D33_15385 D9E49_19020 D9I20_10460 D9J46_03345 DNR41_00375 DS966_16070 DU333_03260 DW236_02290 ECTO124_02024 EGT48_04930 EPS76_06485 ERS085406_02591 NCTC10766_03778 NCTC7928_05955 NCTC8450_02317 NCTC9007_02951 NCTC9075_02834 NCTC9775_01269 SY51_11150] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[RIP1 YEL024W] Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 7.1.1.8) (Complex III subunit 5) (Rieske iron-sulfur protein) (RISP) (Ubiquinol-cytochrome c reductase iron-sulfur subunit)
[Cyp2b10 Cyp2b-10 Cyp2b20] Cytochrome P450 2B10 (EC 1.14.14.1) (CYPIIB10) (CYPIIB20) (Cytochrome P450 2B20) (Cytochrome P450 clone PF3/46) (Cytochrome P450-16-alpha) (P24) (Testosterone 16-alpha hydroxylase)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CQP61_17160 CRD98_26150 CY655_12940 D5618_21870 D8K42_21280 D8Y29_11125 D9D20_21030 D9D43_06110 D9E22_21005 D9H68_20750 D9H70_25730 D9I87_15275 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTM25_06080 DU321_04440 E2855_02503 E2863_02392 EC95NR1_00961 ED648_25045 EFV01_02465 EFV04_09725 EOL36_23890 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9112_02079 NCTC9703_00277 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[cypD cyp102A2 yetO yfnJ BSU07250] Bifunctional cytochrome P450/NADPH--P450 reductase 1 (CYP102A2) (Fatty acid hydroxylase CypD) (Flavocytochrome P450 102A2) [Includes: Cytochrome P450 102A2 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]
[COX2 OXI1 Q0250] Cytochrome c oxidase subunit 2 (EC 1.9.3.1) (Cytochrome c oxidase polypeptide II)
[Or22a AN11 DOR22A.1 dor53 Or22A.1 CG12193] Odorant receptor 22a
[Cyp18a1 CYP18 Eig17-1 CG6816] Cytochrome P450 18a1 (EC 1.14.-.-) (CYPXVIIIA1)
[cyc-1 cyt-12 B1K11.020 NCU01808] Cytochrome c
[phm Cyp306a1 CG6578] Cytochrome P450 306a1 (CYPCCCVIA1) (EC 1.14.-.-) (Protein phantom) (Dmphm)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[AI4 ENS2 I-SCEII Q0065] Intron-encoded DNA endonuclease aI4 (DNA endonuclease I-SceII) [Cleaved into: Truncated non-functional cytochrome oxidase 1; DNA endonuclease aI4 (EC 3.1.-.-) (Intron-encoded endonuclease I-SceII)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[Cyp1b1 Cyp1-b1] Cytochrome P450 1B1 (EC 1.14.14.-) (CYPIB1) (Cytochrome P450CMEF) (Cytochrome P450EF) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152)
[CYT1 CTC1 YOR065W YOR29-16] Cytochrome c1, heme protein, mitochondrial (Complex III subunit 4) (Complex III subunit IV) (Cytochrome b-c1 complex subunit 4) (Ubiquinol-cytochrome-c reductase complex cytochrome c1 subunit) (Cytochrome c-1)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[Cyb5r4 Ncb5or] Cytochrome b5 reductase 4 (EC 1.6.2.2) (Flavohemoprotein b5/b5R) (b5+b5R) (N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein) (cb5/cb5R)
[CYB5R4 NCB5OR] Cytochrome b5 reductase 4 (EC 1.6.2.2) (Flavohemoprotein b5/b5R) (b5+b5R) (N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein) (cb5/cb5R)
[AHK4 CRE1 RAW1 WOL At2g01830 T23K3.2] Histidine kinase 4 (EC 2.7.13.3) (Arabidopsis histidine kinase 4) (AtHK4) (Cytokinin receptor CYTOKININ RESPONSE 1) (AtCRE1) (Cytokinin receptor CRE1) (Phosphoprotein phosphatase AHK4) (EC 3.1.3.16) (Protein AUTHENTIC HIS-KINASE 4) (Protein ROOT AS IN WOL 1) (Protein WOODEN LEG)

Bibliography :
[30198888] Serendipitous crystallization and structure determination of bacterioferritin from Achromobacter.
[28914315] Tyr25, Tyr58 and Trp133 of Escherichia coli bacterioferritin transfer electrons between iron in the central cavity and the ferroxidase centre.
[23167635] Protein dynamics and ion traffic in bacterioferritin.
[21574546] Two distinct ferritin-like molecules in Pseudomonas aeruginosa: the product of the bfrA gene is a bacterial ferritin (FtnA) and not a bacterioferritin (Bfr).
[21106523] A new role for heme, facilitating release of iron from the bacterioferritin iron biomineral.
[20067302] Structural studies of bacterioferritin B from Pseudomonas aeruginosa suggest a gating mechanism for iron uptake via the ferroxidase center .
[19946376] Crystal structure of Bfr A from Mycobacterium tuberculosis: incorporation of selenomethionine results in cleavage and demetallation of haem.
[19391621] Structural basis for iron mineralization by bacterioferritin.
[9409768] Evidence for two types of subunits in the bacterioferritin of Magnetospirillum magnetotacticum.
[8526846] Identification of the ferroxidase centre of Escherichia coli bacterioferritin.