位置:首页 > 蛋白库 > FER_BACTH
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.;
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024