FER_BACTH
ID FER_BACTH Reviewed; 81 AA.
AC P10245;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ferredoxin;
OS Bacillus thermoproteolyticus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1427;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=3351918; DOI=10.1016/0022-2836(88)90388-9;
RA Fukuyama K., Nagahara Y., Tsukihara T., Katsube Y., Hase T., Matsubara H.;
RT "Tertiary structure of Bacillus thermoproteolyticus [4Fe-4S] ferredoxin.
RT Evolutionary implications for bacterial ferredoxins.";
RL J. Mol. Biol. 199:183-193(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=2600971; DOI=10.1016/0022-2836(89)90338-0;
RA Fukuyama K., Matsubara H., Tsukihara T., Katsube Y.;
RT "Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined
RT at 2.3-A resolution. Structural comparisons of bacterial ferredoxins.";
RL J. Mol. Biol. 210:383-398(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (0.92 ANGSTROMS).
RX PubMed=11827483; DOI=10.1006/jmbi.2001.5292;
RA Fukuyama K., Okada T., Kakuta Y., Takahashi Y.;
RT "Atomic resolution structures of oxidized [4Fe-4S] ferredoxin from Bacillus
RT thermoproteolyticus in two crystal forms: systematic distortion of [4Fe-4S]
RT cluster in the protein.";
RL J. Mol. Biol. 315:1155-1166(2002).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster.;
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DR PIR; A55790; A55790.
DR PDB; 1IQZ; X-ray; 0.92 A; A=1-81.
DR PDB; 1IR0; X-ray; 1.00 A; A=1-81.
DR PDB; 1WTF; X-ray; 1.60 A; A/B/C/D=1-81.
DR PDBsum; 1IQZ; -.
DR PDBsum; 1IR0; -.
DR PDBsum; 1WTF; -.
DR AlphaFoldDB; P10245; -.
DR SMR; P10245; -.
DR EvolutionaryTrace; P10245; -.
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:0005506; F:iron ion binding; IEA:InterPro.
DR InterPro; IPR001080; 3Fe4S_ferredoxin.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR PRINTS; PR00352; 3FE4SFRDOXIN.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Transport.
FT CHAIN 1..81
FT /note="Ferredoxin"
FT /id="PRO_0000159192"
FT DOMAIN 2..30
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1IQZ"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:1IQZ"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:1IQZ"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:1IQZ"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1IQZ"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1IQZ"
FT TURN 36..40
FT /evidence="ECO:0007829|PDB:1IQZ"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1IQZ"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:1IQZ"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1IQZ"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:1IQZ"
SQ SEQUENCE 81 AA; 8770 MW; C44C3D9B193A525C CRC64;
PKYTIVDKET CIACGACGAA APDIYDYDED GIAYVTLDDN QGIVEVPDIL IDDMMDAFEG
CPTDSIKVAD EPFDGDPNKF E