ID F0Z3F2_9CLOT Unreviewed; 56 AA.
AC F0Z3F2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU365098};
GN ORFNames=HMPREF0240_03644 {ECO:0000313|EMBL:EGB91584.1};
OS Clostridium sp. D5.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=556261 {ECO:0000313|EMBL:EGB91584.1, ECO:0000313|Proteomes:UP000003978};
RN [1] {ECO:0000313|EMBL:EGB91584.1, ECO:0000313|Proteomes:UP000003978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D5 {ECO:0000313|EMBL:EGB91584.1,
RC ECO:0000313|Proteomes:UP000003978};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., White A.P., Crowley S., Surette M.G., Strauss J.C.,
RA Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium sp. D5.";
RL Submitted (MAR-2010) 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU365098};
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DR EMBL; GL870817; EGB91584.1; -; Genomic_DNA.
DR RefSeq; WP_009004931.1; NZ_GL870817.1.
DR AlphaFoldDB; F0Z3F2; -.
DR eggNOG; COG1148; Bacteria.
DR HOGENOM; CLU_139698_11_4_9; -.
DR OrthoDB; 9803397at2; -.
DR Proteomes; UP000003978; Unassembled WGS sequence.
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; PF13187; Fer4_9; 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; 2.
PE 4: Predicted;
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:UP000003978};
KW Transport {ECO:0000256|RuleBase:RU365098}.
FT DOMAIN 1..28
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 29..56
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 56 AA; 5557 MW; 51F94C0F72D55711 CRC64;
MAHFINDECV SCGSCEGECP VGAIAEGDGK YVIDADACVD CGACEGACPT GAIQAE
//
