ID   FER_CLOAC               Reviewed;          55 AA.
AC   P00198;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   16-JUN-2009, entry version 78.
DE   RecName: Full=Ferredoxin;
OS   Clostridium acidi-urici.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1556;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=69253175; PubMed=5799135; DOI=10.1021/bi00834a035;
RA   Rall S.C., Bolinger R.E., Cole R.D.;
RT   "The amino acid sequence of ferredoxin from Clostridium acidi-urici.";
RL   Biochemistry 8:2486-2496(1969).
RN   [2]
RP   SEQUENCE REVISION TO 15; 21; 25 AND 28.
RC   STRAIN=ATCC 7906 / CIP 104303 / DSM 604 / NCCB 46094 / 9a;
RX   MEDLINE=93384542; PubMed=8373379;
RA   Meyer J., Moulis J.-M., Scherrer N., Gagnon J., Ulrich J.;
RT   "Sequences of clostridial ferredoxins: determination of the
RT   Clostridium sticklandii sequence and correction of the Clostridium
RT   acidurici sequence.";
RL   Biochem. J. 294:622-623(1993).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS).
RX   MEDLINE=95055710; PubMed=7966291; DOI=10.1016/0022-2836(94)90041-8;
RA   Duee E.D., Fanchon E., Vicat J., Sieker L.C., Meyer J., Moulis J.-M.;
RT   "Refined crystal structure of the 2[4Fe-4S] ferredoxin from
RT   Clostridium acidurici at 1.84-A resolution.";
RL   J. Mol. Biol. 243:683-695(1994).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (0.94 ANGSTROMS).
RX   MEDLINE=98070231; PubMed=9405040; DOI=10.1021/bi972155y;
RA   Dauter Z., Wilson K.S., Sieker L.C., Meyer J., Moulis J.-M.;
RT   "Atomic resolution (0.94 A) structure of Clostridium acidurici
RT   ferredoxin. Detailed geometry of [4Fe-4S] clusters in a protein.";
RL   Biochemistry 36:16065-16073(1997).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer
CC       electrons in a wide variety of metabolic reactions.
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters.
CC   -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
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DR   PIR; S36790; FECLCU.
DR   PDB; 1FCA; X-ray; 1.80 A; A=1-55.
DR   PDB; 1FDN; X-ray; 1.84 A; A=1-55.
DR   PDB; 2FDN; X-ray; 0.94 A; A=1-55.
DR   PDBsum; 1FCA; -.
DR   PDBsum; 1FDN; -.
DR   PDBsum; 2FDN; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR001450; 4Fe4S_Fe_S_bd_subgr.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR000813; 7Fe_ferredoxin.
DR   Pfam; PF00037; Fer4; 2.
DR   PRINTS; PR00354; 7FE8SFRDOXIN.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport;
KW   Iron; Iron-sulfur; Metal-binding; Repeat; Transport.
FT   CHAIN         1     55       Ferredoxin.
FT                                /FTId=PRO_0000159109.
FT   DOMAIN        2     27       4Fe-4S ferredoxin-type 1.
FT   DOMAIN       28     55       4Fe-4S ferredoxin-type 2.
FT   METAL         8      8       Iron-sulfur 1 (4Fe-4S).
FT   METAL        11     11       Iron-sulfur 1 (4Fe-4S).
FT   METAL        14     14       Iron-sulfur 1 (4Fe-4S).
FT   METAL        18     18       Iron-sulfur 2 (4Fe-4S).
FT   METAL        37     37       Iron-sulfur 2 (4Fe-4S).
FT   METAL        40     40       Iron-sulfur 2 (4Fe-4S).
FT   METAL        43     43       Iron-sulfur 2 (4Fe-4S).
FT   METAL        47     47       Iron-sulfur 1 (4Fe-4S).
FT   STRAND        2      4
FT   HELIX        15     17
FT   STRAND       27     29
FT   TURN         34     36
FT   HELIX        42     45
FT   STRAND       52     54
SQ   SEQUENCE   55 AA;  5539 MW;  D038C1364A1E97E6 CRC64;
     AYVINEACIS CGACEPECPV NAISSGDDRY VIDADTCIDC GACAGVCPVD APVQA
//