ID   FER5_AQUAE              Reviewed;          96 AA.
AC   P59799;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=2Fe-2S ferredoxin-5;
DE            Short=Fd5;
GN   Name=fdx5; OrderedLocusNames=aq_659;
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   IDENTIFICATION, PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX   PubMed=12564939; DOI=10.1021/bi027116n;
RA   Mitou G., Higgins C., Wittung-Stafshede P., Conover R.C., Smith A.D.,
RA   Johnson M.K., Gaillard J., Stubna A., Muenck E., Meyer J.;
RT   "An Isc-type extremely thermostable [2Fe-2S] ferredoxin from Aquifex
RT   aeolicus. Biochemical, spectroscopic, and unfolding studies.";
RL   Biochemistry 42:1354-1364(2003).
CC   -!- FUNCTION: May be involved in the assembly of iron-sulfur clusters (Isc-
CC       Fd).
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is -390 mV.;
CC       Temperature dependence:
CC         Optimum temperature is 106 degrees Celsius at pH 7. Highly
CC         thermostable.;
CC   -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A59444; A59444.
DR   AlphaFoldDB; P59799; -.
DR   SMR; P59799; -.
DR   InParanoid; P59799; -.
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   GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
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; IPR001055; Adrenodoxin.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   PANTHER; PTHR23426; PTHR23426; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..96
FT                   /note="2Fe-2S ferredoxin-5"
FT                   /id="PRO_0000201181"
FT   DOMAIN          2..96
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         36
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         42
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         45
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         81
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   96 AA;  10537 MW;  0C4F848954F13EE0 CRC64;
     MPKVIVANIN AEFEGIENET IMQILYRNGI EIDSACGGHG QCTSCKVLII SGSENLYPAE
     FEEKDTLEEN GMDPETERLS CQAKLNGKGD VVIYLP