ID E0SSP4_IGNAA Unreviewed; 76 AA.
AC E0SSP4;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU368020};
GN OrderedLocusNames=Igag_1832 {ECO:0000313|EMBL:ADM28629.1};
OS Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignisphaera.
OX NCBI_TaxID=583356 {ECO:0000313|EMBL:ADM28629.1, ECO:0000313|Proteomes:UP000001304};
RN [1] {ECO:0000313|EMBL:ADM28629.1, ECO:0000313|Proteomes:UP000001304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17230 / JCM 13409 / AQ1.S1
RC {ECO:0000313|Proteomes:UP000001304};
RX PubMed=21304693; DOI=10.4056/sigs.1072907;
RA Goker M., Held B., Lapidus A., Nolan M., Spring S., Yasawong M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Tapia R., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Brambilla E., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Sikorski J.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ignisphaera aggregans type strain (AQ1.S1).";
RL Stand. Genomic Sci. 3:66-75(2010).
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP002098; ADM28629.1; -; Genomic_DNA.
DR AlphaFoldDB; E0SSP4; -.
DR STRING; 583356.Igag_1832; -.
DR KEGG; iag:Igag_1832; -.
DR HOGENOM; CLU_139698_9_1_2; -.
DR BioCyc; IAGG583356:GHAH-1820-MONOMER; -.
DR Proteomes; UP000001304; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000001304};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368020}.
FT DOMAIN 2..30
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 35..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 76 AA; 8152 MW; 8BB142F3B72A9B1A CRC64;
MAQVKVNKET CIACGVCWAL VPDVFELDPA TGKTRIRDPY RKSDTETESV GEIPDNLVEP
SKNAAASCPT GSIVVE
//
