ID   FER_MEGGA               Reviewed;          58 AA.
AC   P00209;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Ferredoxin-2;
DE   AltName: Full=Ferredoxin II;
DE            Short=FdII;
OS   Megalodesulfovibrio gigas (Desulfovibrio gigas).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Megalodesulfovibrio.
OX   NCBI_TaxID=879;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=518659; DOI=10.1016/0006-291x(79)91567-5;
RA   Bruschi M.;
RT   "Amino acid sequence of Desulfovibrio gigas ferredoxin: revisions.";
RL   Biochem. Biophys. Res. Commun. 91:623-628(1979).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=4946273; DOI=10.1016/0006-291x(71)90840-0;
RA   Travis J., Newman D.J., le Gall J., Peck H.D. Jr.;
RT   "The amino acid sequence of ferredoxin from the sulfate reducing bacterium,
RT   Desulfovibrio gigas.";
RL   Biochem. Biophys. Res. Commun. 45:452-458(1971).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SEQUENCE REVISION, METHYLTHIOLATION
RP   AT CYS-11, AND DISULFIDE BOND.
RX   PubMed=2920839; DOI=10.1016/0014-5793(89)80580-0;
RA   Kissinger C.R., Adman E.T., Sieker L.C., Jensen L.H., le Gall J.;
RT   "The crystal structure of the three-iron ferredoxin II from Desulfovibrio
RT   gigas.";
RL   FEBS Lett. 244:447-450(1989).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   PubMed=2056535; DOI=10.1016/0022-2836(91)90665-s;
RA   Kissinger C.R., Sieker L.C., Adman E.T., Jensen L.H.;
RT   "Refined crystal structure of ferredoxin II from Desulfovibrio gigas at 1.7
RT   A.";
RL   J. Mol. Biol. 219:693-715(1991).
RN   [5]
RP   STRUCTURE BY NMR.
RX   PubMed=10555576; DOI=10.1007/s007750050328;
RA   Goodfellow B.J., Macedo A.L., Rodrigues P., Moura I., Wray V., Moura J.J.;
RT   "The solution structure of a [3Fe-4S] ferredoxin: oxidised ferredoxin II
RT   from Desulfovibrio gigas.";
RL   J. Biol. Inorg. Chem. 4:421-430(1999).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions.
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC       Note=Binds 1 [3Fe-4S] cluster in its tetrameric form.;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster in its dimeric form.;
CC   -!- SUBUNIT: Homodimer (ferredoxin I) or homotetramer (ferredoxin II).
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DR   PIR; S48666; FEDVFG.
DR   PDB; 1F2G; NMR; -; A=1-58.
DR   PDB; 1FXD; X-ray; 1.70 A; A=1-58.
DR   PDBsum; 1F2G; -.
DR   PDBsum; 1FXD; -.
DR   AlphaFoldDB; P00209; -.
DR   SMR; P00209; -.
DR   EvolutionaryTrace; P00209; -.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   InterPro; IPR001080; 3Fe4S_ferredoxin.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   PRINTS; PR00352; 3FE4SFRDOXIN.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; 3Fe-4S; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Iron; Iron-sulfur; Metal-binding; Methylation; Repeat;
KW   Transport.
FT   CHAIN           1..58
FT                   /note="Ferredoxin-2"
FT                   /id="PRO_0000159195"
FT   DOMAIN          2..27
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          30..58
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         8
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT   BINDING         14
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT   BINDING         50
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT   MOD_RES         11
FT                   /note="Cysteine methyl disulfide"
FT                   /evidence="ECO:0000269|PubMed:2920839"
FT   DISULFID        18..42
FT                   /evidence="ECO:0000269|PubMed:2920839"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:1FXD"
FT   TURN            5..7
FT                   /evidence="ECO:0007829|PDB:1F2G"
FT   HELIX           13..17
FT                   /evidence="ECO:0007829|PDB:1FXD"
FT   TURN            19..21
FT                   /evidence="ECO:0007829|PDB:1FXD"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:1FXD"
FT   STRAND          26..34
FT                   /evidence="ECO:0007829|PDB:1FXD"
FT   HELIX           41..49
FT                   /evidence="ECO:0007829|PDB:1FXD"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:1FXD"
SQ   SEQUENCE   58 AA;  6262 MW;  A479B524E828CD71 CRC64;
     PIEVNDDCMA CEACVEICPD VFEMNEEGDK AVVINPDSDL DCVEEAIDSC PAEAIVRS