ID D4GCI2_PANAM Unreviewed; 163 AA.
AC D4GCI2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Bacterioferritin {ECO:0000256|ARBA:ARBA00019061, ECO:0000256|PIRNR:PIRNR002560};
DE EC=1.16.3.1 {ECO:0000256|PIRNR:PIRNR002560};
GN Name=bfr {ECO:0000313|EMBL:ADD78793.1};
GN OrderedLocusNames=PANA_3626 {ECO:0000313|EMBL:ADD78793.1};
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD78793.1, ECO:0000313|Proteomes:UP000001702};
RN [1] {ECO:0000313|EMBL:ADD78793.1, ECO:0000313|Proteomes:UP000001702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD78793.1,
RC ECO:0000313|Proteomes:UP000001702};
RX PubMed=20348253; DOI=10.1128/JB.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(2010).
CC -!- FUNCTION: Iron-storage protein, whose ferroxidase center binds Fe(2+)
CC ions, oxidizes them by dioxygen to Fe(3+), and participates in the
CC subsequent Fe(3+) oxide mineral core formation within the central
CC cavity of the protein complex. {ECO:0000256|PIRNR:PIRNR002560}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR002560};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SIMILARITY: Belongs to the bacterioferritin family.
CC {ECO:0000256|ARBA:ARBA00008093, ECO:0000256|PIRNR:PIRNR002560}.
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DR EMBL; CP001875; ADD78793.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GCI2; -.
DR STRING; 706191.PANA_3626; -.
DR KEGG; pam:PANA_3626; -.
DR eggNOG; COG2193; Bacteria.
DR HOGENOM; CLU_104506_2_0_6; -.
DR Proteomes; UP000001702; Chromosome.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR CDD; cd00907; Bacterioferritin; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR002024; Bacterioferritin.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR NCBIfam; TIGR00754; bfr; 1.
DR PANTHER; PTHR30295; BACTERIOFERRITIN; 1.
DR PANTHER; PTHR30295:SF0; BACTERIOFERRITIN; 1.
DR Pfam; PF00210; Ferritin; 1.
DR PIRSF; PIRSF002560; Bacterioferritin; 1.
DR PRINTS; PR00601; BACFERRITIN.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR002560};
KW Iron {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|PIRSR:PIRSR002560-1};
KW Iron storage {ECO:0000256|PIRNR:PIRNR002560};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR002560,
KW ECO:0000256|PIRSR:PIRSR002560-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001702}.
FT DOMAIN 7..151
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
FT BINDING 24
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 52
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 56
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 58
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_note="ligand shared between dimeric partners"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 100
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
FT BINDING 136
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
SQ SEQUENCE 163 AA; 19098 MW; C4E4C8C0F80F4E5B CRC64;
MSGGREMKGD AKIISHLNKL LGNELVAINQ YFLHARMFKN WGLMRLNDVE YHESIDEMKH
ADKYIERILF LEGIPNLQDL GRLRVGEDVE EMLQSDLNLE LEGAKDLREA IAYADKIHDY
VSRDMMIEIL ADEEHHIDWI ETELDLIKKM GIQNYLQAQI RDE
//
