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Database: UniProt
Entry: F0H2J7_9FIRM
LinkDB: F0H2J7_9FIRM
Original site: F0H2J7_9FIRM 
ID   F0H2J7_9FIRM            Unreviewed;        58 AA.
AC   F0H2J7;
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=HMPREF9246_0038 {ECO:0000313|EMBL:EGC83280.1};
OS   Anaerococcus hydrogenalis ACS-025-V-Sch4.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Anaerococcus.
OX   NCBI_TaxID=879306 {ECO:0000313|EMBL:EGC83280.1, ECO:0000313|Proteomes:UP000005277};
RN   [1] {ECO:0000313|EMBL:EGC83280.1, ECO:0000313|Proteomes:UP000005277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-025-V-Sch4 {ECO:0000313|EMBL:EGC83280.1,
RC   ECO:0000313|Proteomes:UP000005277};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JAN-2011) 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};
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:EGC83280.1}.
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DR   EMBL; AEXN01000037; EGC83280.1; -; Genomic_DNA.
DR   RefSeq; WP_004813856.1; NZ_AEXN01000037.1.
DR   AlphaFoldDB; F0H2J7; -.
DR   GeneID; 84578144; -.
DR   OrthoDB; 9803397at2; -.
DR   Proteomes; UP000005277; 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; PTHR43687; ADENYLYLSULFATE REDUCTASE, BETA SUBUNIT; 1.
DR   PANTHER; PTHR43687:SF1; L-ASPARTATE SEMIALDEHYDE SULFURTRANSFERASE IRON-SULFUR SUBUNIT; 1.
DR   Pfam; PF14697; Fer4_21; 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}; Transport {ECO:0000256|RuleBase:RU365098}.
FT   DOMAIN          1..29
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          30..58
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   58 AA;  6021 MW;  69CCF4F73B88AC3E CRC64;
     MAYRIDENTC ISCGSCEGEC PVQAIEQGDA AYEIDEDACI DCGSCAAVCP VEAISPAE
//
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