ID   FDXN_RHOCB              Reviewed;          65 AA.
AC   D5ARY6; P16021;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Ferredoxin-1;
DE   AltName: Full=Ferredoxin I;
DE            Short=FdI;
GN   Name=fdxN; OrderedLocusNames=RCAP_rcc03284;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=2315024; DOI=10.1093/nar/18.4.1060;
RA   Saeki K., Miyatake Y., Young D.A., Marrs B., Matsubara H.;
RT   "A plant-ferredoxin-like gene is located upstream of ferredoxin I gene
RT   (fdxN) of Rhodobacter capsulatus.";
RL   Nucleic Acids Res. 18:1060-1060(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-65.
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=2277040; DOI=10.1093/oxfordjournals.jbchem.a123224;
RA   Saeki K., Suetsugu Y., Yao Y., Horio T., Marrs B.L., Matsubara H.;
RT   "Two distinct ferredoxins from Rhodobacter capsulatus: complete amino acid
RT   sequences and molecular evolution.";
RL   J. Biochem. 108:475-482(1990).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions. This ferredoxin probably
CC       participates in nitrogen fixation.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 2 [4Fe-4S] clusters. {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; X51316; CAA35699.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE87008.1; -; Genomic_DNA.
DR   PIR; A33498; FERF1C.
DR   RefSeq; WP_013068980.1; NC_014034.1.
DR   AlphaFoldDB; D5ARY6; -.
DR   SMR; D5ARY6; -.
DR   STRING; 272942.RCAP_rcc03284; -.
DR   EnsemblBacteria; ADE87008; ADE87008; RCAP_rcc03284.
DR   GeneID; 31492064; -.
DR   KEGG; rcp:RCAP_rcc03284; -.
DR   eggNOG; COG1145; Bacteria.
DR   HOGENOM; CLU_139698_11_0_5; -.
DR   OMA; CGDCKPV; -.
DR   OrthoDB; 1873445at2; -.
DR   Proteomes; UP000002361; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   Pfam; PF00037; Fer4; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Nitrogen fixation; Reference proteome; Repeat; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2277040"
FT   CHAIN           2..65
FT                   /note="Ferredoxin-1"
FT                   /id="PRO_0000410435"
FT   DOMAIN          2..30
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         10
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         20
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   65 AA;  6864 MW;  2DF359B3BC3E481E CRC64;
     MAMKIDPELC TSCGDCEPVC PTNAIAPKKG VYVINADTCT ECEGEHDLPQ CVNACMTDNC
     INPAA