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Database: UniProt
Entry: L8DGC5_9NOCA
LinkDB: L8DGC5_9NOCA
Original site: L8DGC5_9NOCA 
ID   L8DGC5_9NOCA            Unreviewed;        65 AA.
AC   L8DGC5;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU368020};
GN   ORFNames=RHODMAR_0335 {ECO:0000313|EMBL:CCQ13703.1};
OS   Rhodococcus sp. AW25M09.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1268303 {ECO:0000313|EMBL:CCQ13703.1, ECO:0000313|Proteomes:UP000011207};
RN   [1] {ECO:0000313|EMBL:CCQ13703.1, ECO:0000313|Proteomes:UP000011207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AW25M09 {ECO:0000313|EMBL:CCQ13703.1,
RC   ECO:0000313|Proteomes:UP000011207};
RA   Hjerde E., Pierechod M.M., Williamson A.K., Bjerga G., Willassen N.P.,
RA   Smalaas A.O., Altermark B.;
RT   "Draft genome sequence of Rhodococcus sp. AW25M09. An Actinomycete isolated
RT   from Atlantic Hagfish caught in Hadselfjorden, North- Norway.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions.
CC       {ECO:0000256|RuleBase:RU368020}.
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|ARBA:ARBA00001927};
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:CCQ13703.1}.
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DR   EMBL; CAPS01000010; CCQ13703.1; -; Genomic_DNA.
DR   RefSeq; WP_008710625.1; NZ_CAPS01000010.1.
DR   AlphaFoldDB; L8DGC5; -.
DR   STRING; 1268303.RHODMAR_0335; -.
DR   eggNOG; COG1141; Bacteria.
DR   OrthoDB; 3215002at2; -.
DR   Proteomes; UP000011207; Unassembled WGS sequence.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.20; -; 1.
DR   InterPro; IPR001080; 3Fe4S_ferredoxin.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   PANTHER; PTHR36923; FERREDOXIN; 1.
DR   PANTHER; PTHR36923:SF3; FERREDOXIN; 1.
DR   Pfam; PF13459; Fer4_15; 1.
DR   PRINTS; PR00352; 3FE4SFRDOXIN.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU368020};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU368020};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU368020};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368020};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368020}.
FT   DOMAIN          1..29
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   65 AA;  6906 MW;  2D81DCBD711D142B CRC64;
     MKIDVDWERC EGHGICAEQA PKVFSLDDEG ELHHAFDGQE IPDDLAASAR SAVGVCPVAA
     LKAQG
//
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