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FER1_DESAF
ID   FER1_DESAF              Reviewed;          65 AA.
AC   P00210;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Ferredoxin-1;
DE   AltName: Full=Ferredoxin I;
DE            Short=FdI;
GN   Name=fd1;
OS   Desulfocurvibacter africanus (Desulfovibrio africanus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfocurvibacter.
OX   NCBI_TaxID=873;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi;
RA   Cavazza C.C., Hatchikian E.C.;
RT   "Investigations of the role of surface residues of ferredoxin I from
RT   Desulfovibrio africanus in the interaction with its redox partner, the
RT   pyruvate ferredoxin:oxidoreductase.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-65.
RC   STRAIN=ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi;
RX   PubMed=7126685; DOI=10.1016/s0300-9084(82)80166-1;
RA   Bruschi M., Hatchikian E.C.;
RT   "Non-heme iron proteins of Desulfovibrio: the primary structure of
RT   ferredoxin I from Desulfovibrio africanus.";
RL   Biochimie 64:503-507(1982).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SEQUENCE REVISION.
RX   PubMed=7803404; DOI=10.1021/bi00255a022;
RA   Seri A., Housset D., Serre L., Bonicel J., Hatchikian E.C., Frey M.,
RA   Roth M.;
RT   "Crystal structure of the ferredoxin I from Desulfovibrio africanus at 2.3-
RT   A resolution.";
RL   Biochemistry 33:15408-15417(1994).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=9533888; DOI=10.1006/jmbi.1998.1631;
RA   Davy S.L., Osborne M.J., Moore G.R.;
RT   "Determination of the structure of oxidised Desulfovibrio africanus
RT   ferredoxin I by 1H NMR spectroscopy and comparison of its solution
RT   structure with its crystal structure.";
RL   J. Mol. Biol. 277:683-706(1998).
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   -!- SUBUNIT: Homodimer.
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DR   EMBL; AJ489482; CAD33799.1; -; Genomic_DNA.
DR   PIR; A56050; FEDV1A.
DR   PDB; 1DAX; NMR; -; A=2-65.
DR   PDB; 1DFD; NMR; -; A=2-65.
DR   PDB; 1FXR; X-ray; 2.30 A; A/B=2-65.
DR   PDBsum; 1DAX; -.
DR   PDBsum; 1DFD; -.
DR   PDBsum; 1FXR; -.
DR   AlphaFoldDB; P00210; -.
DR   SMR; P00210; -.
DR   EvolutionaryTrace; P00210; -.
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; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7126685"
FT   CHAIN           2..65
FT                   /note="Ferredoxin-1"
FT                   /id="PRO_0000159194"
FT   DOMAIN          3..31
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         12
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:7803404"
FT   BINDING         15
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:7803404"
FT   BINDING         18
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:7803404"
FT   BINDING         55
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:7803404"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:1FXR"
FT   TURN            9..11
FT                   /evidence="ECO:0007829|PDB:1FXR"
FT   HELIX           17..21
FT                   /evidence="ECO:0007829|PDB:1FXR"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:1FXR"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:1FXR"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:1FXR"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:1FXR"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:1DAX"
FT   HELIX           45..54
FT                   /evidence="ECO:0007829|PDB:1FXR"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:1DAX"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:1FXR"
SQ   SEQUENCE   65 AA;  7333 MW;  2B48BF6C20353D93 CRC64;
     MARKFYVDQD ECIACESCVE IAPGAFAMDP EIEKAYVKDV EGASQEEVEE AMDTCPVQCI
     HWEDE
 
 
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