FER1_AQUAE
ID FER1_AQUAE Reviewed; 96 AA.
AC O67065;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ferredoxin-1;
DE Short=Fd1;
GN Name=fdx1; OrderedLocusNames=aq_919.1; ORFNames=aq_919A;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP DISULFIDE BOND.
RX PubMed=11863449; DOI=10.1021/bi015981m;
RA Meyer J., Clay M.D., Johnson M.K., Stubna A., Munck E., Higgins C.,
RA Wittung-Stafshede P.;
RT "A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus
RT is stabilized by a disulfide bond.";
RL Biochemistry 41:3096-3108(2002).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC07010.1; -; Genomic_DNA.
DR PIR; F70379; F70379.
DR RefSeq; NP_213627.1; NC_000918.1.
DR RefSeq; WP_010880565.1; NC_000918.1.
DR AlphaFoldDB; O67065; -.
DR SMR; O67065; -.
DR STRING; 224324.aq_919a; -.
DR EnsemblBacteria; AAC07010; AAC07010; aq_919a.
DR KEGG; aae:aq_919a; -.
DR PATRIC; fig|224324.8.peg.720; -.
DR eggNOG; COG0633; Bacteria.
DR HOGENOM; CLU_082632_8_1_0; -.
DR OMA; GCTDGQC; -.
DR OrthoDB; 1837979at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Disulfide bond; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Transport.
FT CHAIN 1..96
FT /note="Ferredoxin-1"
FT /id="PRO_0000189388"
FT DOMAIN 1..95
FT /note="2Fe-2S ferredoxin-type"
FT BINDING 34
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT DISULFID 52..87
FT /evidence="ECO:0000269|PubMed:11863449"
SQ SEQUENCE 96 AA; 10762 MW; C19592692108C7FC CRC64;
MKVIINGKEF DIPKGVRFGE LSHEIEKAGI EFGCTDGQCG VCVARVIKGM ECLNEPSEEE
EETLWRVGAV DEDQRLTCQL VIEKEDCDEI VIESED
