ID A0A2K8U5Z0_9GAMM Unreviewed; 154 AA.
AC A0A2K8U5Z0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Bacterioferritin {ECO:0000256|ARBA:ARBA00019061, ECO:0000256|PIRNR:PIRNR002560};
DE EC=1.16.3.1 {ECO:0000256|PIRNR:PIRNR002560};
GN ORFNames=THSYN_08615 {ECO:0000313|EMBL:AUB81006.1};
OS Candidatus Thiodictyon syntrophicum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiodictyon.
OX NCBI_TaxID=1166950 {ECO:0000313|EMBL:AUB81006.1, ECO:0000313|Proteomes:UP000232638};
RN [1] {ECO:0000313|EMBL:AUB81006.1, ECO:0000313|Proteomes:UP000232638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cad16T {ECO:0000313|EMBL:AUB81006.1,
RC ECO:0000313|Proteomes:UP000232638};
RA Luedin S.M., Pothier J.F., Danza F., Storelli N., Wittwer M., Tonolla M.;
RT "Complete genome sequence of Candidatus 'Thiodictyon syntrophicum' sp. nov.
RT strain Cad16T, a photolithoautotroph purple sulfur bacterium isolated from
RT an alpine meromictic lake.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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; CP020370; AUB81006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8U5Z0; -.
DR KEGG; tsy:THSYN_08615; -.
DR OrthoDB; 9800505at2; -.
DR Proteomes; UP000232638; 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:UP000232638}.
FT DOMAIN 1..145
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
FT BINDING 52
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 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR002560-1"
SQ SEQUENCE 154 AA; 17442 MW; 8B2BC808203CD8F8 CRC64;
MKTDPSIHQH HNAVLKLALT NINQYFLHAR MLGHWGFKTL EGHAFRASVA VMKEADEVIA
RVLFLEGLPN LQNLGKLLIG EDVPEIIQHD LTAERAYRDA LAAAIGHCET HKDYVSRHEL
EEIQEESEER IDWLETQLAL IAALGLENYL QSAI
//
