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Database: UniProt
Entry: A0A1M3GJ10_9PROT
LinkDB: A0A1M3GJ10_9PROT
Original site: A0A1M3GJ10_9PROT 
ID   A0A1M3GJ10_9PROT        Unreviewed;        69 AA.
AC   A0A1M3GJ10;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Bacterioferritin-associated ferredoxin {ECO:0000256|ARBA:ARBA00039386};
GN   ORFNames=BGO60_14100 {ECO:0000313|EMBL:OJW41529.1};
OS   Thiobacillus sp. 65-1059.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=1895860 {ECO:0000313|EMBL:OJW41529.1, ECO:0000313|Proteomes:UP000184230};
RN   [1] {ECO:0000313|EMBL:OJW41529.1, ECO:0000313|Proteomes:UP000184230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=65-1059 {ECO:0000313|EMBL:OJW41529.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Seems to associate with BFR; could be a general redox and/or
CC       regulatory component participating in the iron storage mobilization
CC       functions of BFR. Could participate in the release or the delivery of
CC       iron from/to bacterioferritin (or other iron complexes).
CC       {ECO:0000256|ARBA:ARBA00037130}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OJW41529.1}.
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DR   EMBL; MKUE01000140; OJW41529.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3GJ10; -.
DR   STRING; 1895860.BGO60_14100; -.
DR   Proteomes; UP000184230; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd19945; Fer2_BFD; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   PANTHER; PTHR37424; BACTERIOFERRITIN-ASSOCIATED FERREDOXIN; 1.
DR   PANTHER; PTHR37424:SF1; BACTERIOFERRITIN-ASSOCIATED FERREDOXIN; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          2..51
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   69 AA;  7442 MW;  CCF65B27D0DAC101 CRC64;
     MYVCLCHSVT DTDIRRLVRT EGVCSMRELS RQLGVATQCG KCGRCAREVL GEALHETRNE
     AGCAALAAA
//
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