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Database: UniProt
Entry: A0A059KI58_9BURK
LinkDB: A0A059KI58_9BURK
Original site: A0A059KI58_9BURK 
ID   A0A059KI58_9BURK        Unreviewed;       101 AA.
AC   A0A059KI58;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Ferredoxin III {ECO:0000256|ARBA:ARBA00030616};
GN   ORFNames=X805_35060 {ECO:0000313|EMBL:KDB50909.1};
OS   Sphaerotilus natans subsp. natans DSM 6575.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Sphaerotilus.
OX   NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB50909.1, ECO:0000313|Proteomes:UP000026714};
RN   [1] {ECO:0000313|EMBL:KDB50909.1, ECO:0000313|Proteomes:UP000026714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB50909.1,
RC   ECO:0000313|Proteomes:UP000026714};
RX   PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA   Park S., Kim D.H., Lee J.H., Hur H.G.;
RT   "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide minerals
RT   formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL   FEMS Microbiol. Ecol. 90:68-77(2014).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions.
CC       {ECO:0000256|ARBA:ARBA00003532}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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:KDB50909.1}.
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DR   EMBL; AZRA01000105; KDB50909.1; -; Genomic_DNA.
DR   RefSeq; WP_037484757.1; NZ_AZRA01000105.1.
DR   AlphaFoldDB; A0A059KI58; -.
DR   STRING; 34103.SAMN05421778_12414; -.
DR   PATRIC; fig|1286631.3.peg.3424; -.
DR   eggNOG; COG1143; Bacteria.
DR   Proteomes; UP000026714; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.20; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR014283; FdIII_4_nif.
DR   NCBIfam; TIGR02936; fdxN_nitrog; 1.
DR   PANTHER; PTHR43687:SF5; 4FE-4S FERREDOXIN-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43687; ADENYLYLSULFATE REDUCTASE, BETA SUBUNIT; 1.
DR   Pfam; PF13484; Fer4_16; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          18..47
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          69..99
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   101 AA;  10930 MW;  CB71FD7C688C9946 CRC64;
     MSTYSVTLPS GATWTPQFVQ SLDEAKCIGC GRCFKVCPRG VLELVGLTED GERISVDLDD
     DDDEAYEKKV MTIAKGELCI GCTACSKICP KKCYTHGAVE V
//
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