ID A0A0N1GKE8_9ACTN Unreviewed; 107 AA.
AC A0A0N1GKE8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ferredoxin {ECO:0000256|ARBA:ARBA00013529, ECO:0000256|RuleBase:RU365098};
GN ORFNames=OK074_0933 {ECO:0000313|EMBL:KPI26264.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI26264.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI26264.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI26264.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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|ARBA:ARBA00003532, ECO:0000256|RuleBase:RU365098}.
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|RuleBase:RU365098};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|RuleBase:RU365098};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU365098};
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:KPI26264.1}.
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DR EMBL; LJCV01000011; KPI26264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1GKE8; -.
DR PATRIC; fig|1592327.3.peg.130; -.
DR OrthoDB; 9803397at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.20; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR000813; 7Fe_ferredoxin.
DR PANTHER; PTHR42859:SF2; FERREDOXIN; 1.
DR PANTHER; PTHR42859; OXIDOREDUCTASE; 1.
DR Pfam; PF00037; Fer4; 1.
DR PRINTS; PR00354; 7FE8SFRDOXIN.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW 3Fe-4S {ECO:0000256|RuleBase:RU365098};
KW 4Fe-4S {ECO:0000256|RuleBase:RU365098};
KW Electron transport {ECO:0000256|RuleBase:RU365098};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365098};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU365098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365098};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW Transport {ECO:0000256|RuleBase:RU365098}.
FT DOMAIN 31..60
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 107 AA; 11895 MW; 20CE04DD0FB850B0 CRC64;
MTYVIAEPCV DVKDKACIEE CPVDCIYEGQ RSLYIHPDEC VDCGACEPVC PVEAIFYEDD
VPEEWKDYYK ANVEYFDELG SPGGASKLGL IERDHPFVAA LPPQGGE
//
