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Database: UniProt
Entry: P20624
LinkDB: P20624
Original site: P20624 
ID   FER3_RHOCA              Reviewed;         101 AA.
AC   P20624;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   13-FEB-2019, entry version 93.
DE   RecName: Full=Ferredoxin-3;
DE   AltName: Full=Ferredoxin III;
DE            Short=FdIII;
GN   Name=fdxB;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2708314; DOI=10.1128/jb.171.5.2591-2598.1989;
RA   Moreno-Vivian C., Hennecke S., Puehler A., Klipp W.;
RT   "Open reading frame 5 (ORF5), encoding a ferredoxinlike protein, and
RT   nifQ are cotranscribed with nifE, nifN, nifX, and ORF4 in Rhodobacter
RT   capsulatus.";
RL   J. Bacteriol. 171:2591-2598(1989).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX   PubMed=8387524;
RA   Jouanneau Y., Meyer C., Gaillard J., Forest E., Gagnon J.;
RT   "Purification and characterization of a novel dimeric ferredoxin
RT   (FdIII) from Rhodobacter capsulatus.";
RL   J. Biol. Chem. 268:10636-10644(1993).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer
CC       electrons in a wide variety of metabolic reactions.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 2 [4Fe-4S] clusters.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA26146.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; M26323; AAA26146.1; ALT_INIT; Genomic_DNA.
DR   PIR; B32308; FERF3C.
DR   RefSeq; WP_023923722.1; NC_014034.1.
DR   PRIDE; P20624; -.
DR   GeneID; 31492055; -.
DR   eggNOG; ENOG4105WCA; Bacteria.
DR   eggNOG; COG1145; LUCA.
DR   BioCyc; GCF_000506425:G1EHH-2495-MONOMER; -.
DR   BioCyc; RCAP272942:G1GUE-3259-MONOMER; -.
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   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR014283; FdIII_4_nif.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   Pfam; PF13237; Fer4_10; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   TIGRFAMs; TIGR02936; fdxN_nitrog; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Nitrogen fixation; Repeat; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    101       Ferredoxin-3.
FT                                /FTId=PRO_0000159189.
FT   DOMAIN       17     46       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       70    100       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        26     26       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        29     29       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        32     32       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        36     36       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        80     80       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        83     83       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        86     86       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        90     90       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   101 AA;  10819 MW;  2F6339AE450C532F CRC64;
     MPTVAYTRGG AEYTPVYLMK IDEQKCIGCG RCFKVCGRDV MSLHGLTEDG QVVAPGTDEW
     DEVEDEIVKK VMALTGAENC IGCGACARVC PSECQTHAAL S
//
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