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Database: UniProt
Entry: P00195
LinkDB: P00195
Original site: P00195 
ID   FER_CLOPA               Reviewed;          56 AA.
AC   P00195;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-DEC-2017, entry version 100.
DE   RecName: Full=Ferredoxin;
OS   Clostridium pasteurianum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3856844; DOI=10.1073/pnas.82.6.1653;
RA   Graves M.C., Mullenbach G.T., Rabinowitz J.C.;
RT   "Cloning and nucleotide sequence determination of the Clostridium
RT   pasteurianum ferredoxin gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:1653-1657(1985).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-56.
RX   PubMed=5335811; DOI=10.1021/bi00869a032;
RA   Tanaka M., Nakashima T., Benson A.M., Mower H.F., Yasunobu K.T.;
RT   "The amino acid sequence of Clostridium pasteurianum ferredoxin.";
RL   Biochemistry 5:1666-1680(1966).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=7556151; DOI=10.1111/j.1432-1033.1995.tb20799.x;
RA   Bertini I., Donaire A., Feinberg B.A., Luchinat C., Piccioli M.,
RA   Yuan H.;
RT   "Solution structure of the oxidized 2[4Fe-4S] ferredoxin from
RT   Clostridium pasteurianum.";
RL   Eur. J. Biochem. 232:192-205(1995).
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.;
DR   EMBL; M11214; AAA83524.1; -; Genomic_DNA.
DR   PIR; A94028; FECLCP.
DR   RefSeq; WP_003440320.1; NZ_LFYL01000002.1.
DR   PDB; 1CLF; NMR; -; A=2-56.
DR   PDBsum; 1CLF; -.
DR   ProteinModelPortal; P00195; -.
DR   SMR; P00195; -.
DR   EvolutionaryTrace; P00195; -.
DR   GO; GO:0051539; F:4 iron, 4 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   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR000813; 7Fe_ferredoxin.
DR   Pfam; PF12838; Fer4_7; 1.
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   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:5335811}.
FT   CHAIN         2     56       Ferredoxin.
FT                                /FTId=PRO_0000159111.
FT   DOMAIN        2     28       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       29     56       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL         9      9       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000269|PubMed:7556151}.
FT   METAL        12     12       Iron-sulfur 1 (4Fe-4S).
FT   METAL        15     15       Iron-sulfur 1 (4Fe-4S).
FT   METAL        19     19       Iron-sulfur 2 (4Fe-4S).
FT   METAL        38     38       Iron-sulfur 2 (4Fe-4S).
FT   METAL        41     41       Iron-sulfur 2 (4Fe-4S).
FT   METAL        44     44       Iron-sulfur 2 (4Fe-4S).
FT   METAL        48     48       Iron-sulfur 1 (4Fe-4S).
FT   TURN         14     18       {ECO:0000244|PDB:1CLF}.
FT   STRAND       24     26       {ECO:0000244|PDB:1CLF}.
FT   STRAND       28     33       {ECO:0000244|PDB:1CLF}.
FT   TURN         35     37       {ECO:0000244|PDB:1CLF}.
FT   TURN         43     47       {ECO:0000244|PDB:1CLF}.
SQ   SEQUENCE   56 AA;  5630 MW;  D74C5AA8D3E7A4EC CRC64;
     MAYKIADSCV SCGACASECP VNAISQGDSI FVIDADTCID CGNCANVCPV GAPVQE
//
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