(data stored in SCRATCH3701 zone)

SWISSPROT: 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   11-DEC-2019, entry version 95.
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:49601; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC       {ECO:0000305}.
DR   EMBL; AJ293319; CAC33744.1; -; Genomic_DNA.
DR   EMBL; AE017197; AAU03673.1; -; Genomic_DNA.
DR   RefSeq; WP_011190660.1; NC_006142.1.
DR   SMR; Q9AKC4; -.
DR   STRING; 257363.RT0189; -.
DR   EnsemblBacteria; AAU03673; AAU03673; RT0189.
DR   KEGG; rty:RT0189; -.
DR   eggNOG; ENOG4108ZIT; Bacteria.
DR   eggNOG; COG0633; LUCA.
DR   HOGENOM; HOG000244518; -.
DR   OMA; SACGGVC; -.
DR   OrthoDB; 1837979at2; -.
DR   BioCyc; RTYP257363:G1G0L-195-MONOMER; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   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;
DR   PRODOM; Q9AKC4.
DR   SWISS-2DPAGE; Q9AKC4.
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   METAL           42
FT                   /note="Iron-sulfur (2Fe-2S)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   METAL           48
FT                   /note="Iron-sulfur (2Fe-2S)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   METAL           51
FT                   /note="Iron-sulfur (2Fe-2S)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   METAL           88
FT                   /note="Iron-sulfur (2Fe-2S)"
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
//

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