FER2_RICTY
ID FER2_RICTY Reviewed; 117 AA.
AC Q9AKC4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=2Fe-2S ferredoxin;
DE AltName: Full=Adrenodoxin-like protein;
GN Name=fdxB; Synonyms=adx1; OrderedLocusNames=RT0189;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=11319266; DOI=10.1093/oxfordjournals.molbev.a003864;
RA Andersson J.O., Andersson S.G.E.;
RT "Pseudogenes, junk DNA, and the dynamics of Rickettsia genomes.";
RL Mol. Biol. Evol. 18:829-839(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
CC -!- FUNCTION: Ferredoxin 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 adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
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DR EMBL; AJ293319; CAC33744.1; -; Genomic_DNA.
DR EMBL; AE017197; AAU03673.1; -; Genomic_DNA.
DR RefSeq; WP_011190660.1; NC_006142.1.
DR AlphaFoldDB; Q9AKC4; -.
DR SMR; Q9AKC4; -.
DR STRING; 257363.RT0189; -.
DR EnsemblBacteria; AAU03673; AAU03673; RT0189.
DR KEGG; rty:RT0189; -.
DR eggNOG; COG0633; Bacteria.
DR HOGENOM; CLU_082632_5_0_5; -.
DR OMA; SACGGVC; -.
DR OrthoDB; 1837979at2; -.
DR Proteomes; UP000000604; 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; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426; PTHR23426; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00814; ADX; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Electron transport; Iron; Iron-sulfur; Metal-binding; Transport.
FT CHAIN 1..117
FT /note="2Fe-2S ferredoxin"
FT /id="PRO_0000201179"
FT DOMAIN 5..107
FT /note="2Fe-2S ferredoxin-type"
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 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 88
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 117 AA; 13075 MW; 30FCD951D643FE07 CRC64;
MLRKIKVTFI INDEEEKTVE APIGLSILEI AHSNNLDLEG ACEGSLACAT CHVMLEEEFY
NKLKKPTEAE EDMLDLAFGL TDTSRLGCQI ILTEELDGIK VRLPSATRNI NYNGFKK
