ID A0A1I4C3K4_9PSEU Unreviewed; 115 AA.
AC A0A1I4C3K4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU365098};
GN ORFNames=SAMN05421835_13226 {ECO:0000313|EMBL:SFK75658.1};
OS Amycolatopsis sacchari.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=115433 {ECO:0000313|EMBL:SFK75658.1, ECO:0000313|Proteomes:UP000199025};
RN [1] {ECO:0000313|EMBL:SFK75658.1, ECO:0000313|Proteomes:UP000199025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44468 {ECO:0000313|EMBL:SFK75658.1,
RC ECO:0000313|Proteomes:UP000199025};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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: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};
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DR EMBL; FORP01000032; SFK75658.1; -; Genomic_DNA.
DR RefSeq; WP_091515713.1; NZ_CBDQZW010000063.1.
DR AlphaFoldDB; A0A1I4C3K4; -.
DR STRING; 115433.SAMN05421835_13226; -.
DR OrthoDB; 9803397at2; -.
DR Proteomes; UP000199025; 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 InterPro; IPR050294; RnfB_subfamily.
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|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU365098};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW 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:UP000199025};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365098}.
FT DOMAIN 31..60
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 72..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 115 AA; 12254 MW; 71E8318265A5937D CRC64;
MPYVIGAQCV DELDGSCVDA CPVDCIYEGA RKRYINPYEC IECGNCLPAC PVDAITAGPP
DAAPEWAEDN KRFFDEPLPG RDEPLESPGG ASLIEPLGVD TELTATIPAR RPDAG
//