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 27-MAR-2024, entry version 83.
DE RecName: Full=2Fe-2S ferredoxin-5;
DE Short=Fd5;
GN Name=fdx5; OrderedLocusNames=aq_659;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificota; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF71; ADRENODOXIN-LIKE PROTEIN 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR23426; FERREDOXIN/ADRENODOXIN; 1.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 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
//
