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Database: UniProt
Entry: I2QVD2_9BRAD
LinkDB: I2QVD2_9BRAD
Original site: I2QVD2_9BRAD 
ID   I2QVD2_9BRAD            Unreviewed;        90 AA.
AC   I2QVD2;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Bacterioferritin-associated ferredoxin {ECO:0000256|ARBA:ARBA00039386};
GN   ORFNames=Bra1253DRAFT_00263 {ECO:0000313|EMBL:EIG63738.1};
OS   Bradyrhizobium sp. WSM1253.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=319003 {ECO:0000313|EMBL:EIG63738.1, ECO:0000313|Proteomes:UP000005125};
RN   [1] {ECO:0000313|EMBL:EIG63738.1, ECO:0000313|Proteomes:UP000005125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1253 {ECO:0000313|EMBL:EIG63738.1,
RC   ECO:0000313|Proteomes:UP000005125};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA   Howieson J., Reeve W., Woyke T.;
RT   "Improved High-Quality Draft sequence of Bradyrhizobium sp. WSM1253.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1253 {ECO:0000313|Proteomes:UP000005125};
RX   PubMed=26629308;
RA   Tiwari R., Howieson J., Yates R., Tian R., Held B., Tapia R., Han C.,
RA   Seshadri R., Reddy T.B., Huntemann M., Pati A., Woyke T., Markowitz V.,
RA   Ivanova N., Kyrpides N., Reeve W.;
RT   "Genome sequence of Bradyrhizobium sp. WSM1253; a microsymbiont of
RT   Ornithopus compressus from the Greek Island of Sifnos.";
RL   Stand. Genomic Sci. 10:113-113(2015).
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}.
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DR   EMBL; JH600072; EIG63738.1; -; Genomic_DNA.
DR   AlphaFoldDB; I2QVD2; -.
DR   eggNOG; COG2906; Bacteria.
DR   HOGENOM; CLU_159205_0_0_5; -.
DR   Proteomes; UP000005125; 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   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          5..57
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   90 AA;  9699 MW;  7AAF4BB682959797 CRC64;
     MRFMIVCSCN VLSDHDVRHA VNTADDAPRN AKQIYDCLGC SAECGRCART IKTIINEAYR
     ECALACQAGC PHSQIMDDAG DEPKVAPAAP
//
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