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Database: UniProt
Entry: P00208
LinkDB: P00208
Original site: P00208 
ID   FER_ALLVD               Reviewed;          83 AA.
AC   P00208; D3RQV5; P71155;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JAN-2019, entry version 120.
DE   RecName: Full=Ferredoxin {ECO:0000305};
DE   AltName: Full=2[4Fe-4S] ferredoxin {ECO:0000303|PubMed:2387857};
GN   Name=fdx; OrderedLocusNames=Alvin_2884;
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 /
OS   NCIMB 10441 / D) (Chromatium vinosum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Allochromatium.
OX   NCBI_TaxID=572477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND COFACTOR.
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=8765743; DOI=10.1016/0167-4781(96)00082-6;
RA   Moulis J.-M.;
RT   "Molecular cloning and expression of the gene encoding Chromatium
RT   vinosum 2[4Fe-4S] ferredoxin.";
RL   Biochim. Biophys. Acta 1308:12-14(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-83.
RX   PubMed=893371;
RA   Hase T., Matsubara H., Evans M.C.W.;
RT   "Amino acid sequence of chromatium vinosum ferredoxin: revisions.";
RL   J. Biochem. 81:1745-1749(1977).
RN   [4]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=2387857;
RA   Smith E.T., Feinberg B.A.;
RT   "Redox properties of several bacterial ferredoxins using square wave
RT   voltammetry.";
RL   J. Biol. Chem. 265:14371-14376(1990).
RN   [5] {ECO:0000244|PDB:1BLU}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-83 IN COMPLEX WITH
RP   IRON-SULFUR (4FE-4S), AND COFACTOR.
RX   PubMed=8880900; DOI=10.1002/pro.5560050902;
RA   Moulis J.-M., Sieker L.C., Wilson K.S., Dauter Z.;
RT   "Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium
RT   vinosum: evolutionary and mechanistic inferences for [3/4Fe-4S]
RT   ferredoxins.";
RL   Protein Sci. 5:1765-1775(1996).
RN   [6] {ECO:0000244|PDB:3EUN, ECO:0000244|PDB:3EXY}
RP   X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 2-83 OF MUTANTS GLY-14 AND
RP   ALA-58 IN COMPLEX WITH IRON-SULFUR (4FE-4S), COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF VAL-14 AND CYS-58.
RX   PubMed=19290553; DOI=10.1007/s00775-009-0492-x;
RA   Saridakis E., Giastas P., Efthymiou G., Thoma V., Moulis J.M.,
RA   Kyritsis P., Mavridis I.M.;
RT   "Insight into the protein and solvent contributions to the reduction
RT   potentials of [4Fe-4S]2+/+ clusters: crystal structures of the
RT   Allochromatium vinosum ferredoxin variants C57A and V13G and the
RT   homologous Escherichia coli ferredoxin.";
RL   J. Biol. Inorg. Chem. 14:783-799(2009).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer
CC       electrons in a wide variety of metabolic reactions.
CC       {ECO:0000305|PubMed:2387857}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:19290553,
CC         ECO:0000269|PubMed:8765743, ECO:0000269|PubMed:8880900};
CC       Note=Binds 2 [4Fe-4S] clusters. {ECO:0000269|PubMed:19290553,
CC       ECO:0000269|PubMed:8765743, ECO:0000269|PubMed:8880900};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is -460 mV (PubMed:2387857). E(0) is -640 mV for the
CC         cluster 1, and -467 mV for the cluster 2 (PubMed:19290553).
CC         {ECO:0000269|PubMed:19290553, ECO:0000269|PubMed:2387857};
DR   EMBL; U45327; AAC44333.1; -; Genomic_DNA.
DR   EMBL; CP001896; ADC63789.1; -; Genomic_DNA.
DR   PIR; S72167; FEKRV.
DR   RefSeq; WP_012972054.1; NC_013851.1.
DR   PDB; 1BLU; X-ray; 2.10 A; A=2-83.
DR   PDB; 3EUN; X-ray; 1.05 A; A=2-83.
DR   PDB; 3EXY; X-ray; 1.48 A; A=2-83.
DR   PDBsum; 1BLU; -.
DR   PDBsum; 3EUN; -.
DR   PDBsum; 3EXY; -.
DR   ProteinModelPortal; P00208; -.
DR   SMR; P00208; -.
DR   STRING; 572477.Alvin_2884; -.
DR   EnsemblBacteria; ADC63789; ADC63789; Alvin_2884.
DR   KEGG; alv:Alvin_2884; -.
DR   eggNOG; ENOG4105K5D; Bacteria.
DR   eggNOG; COG1145; LUCA.
DR   HOGENOM; HOG000044615; -.
DR   OMA; DCCVPDD; -.
DR   OrthoDB; 1873445at2; -.
DR   BioCyc; AVIN572477:G1GHE-2918-MONOMER; -.
DR   EvolutionaryTrace; P00208; -.
DR   Proteomes; UP000001441; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   Pfam; PF00037; Fer4; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; Repeat; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:893371}.
FT   CHAIN         2     83       Ferredoxin.
FT                                /FTId=PRO_0000159127.
FT   DOMAIN        2     29       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       31     64       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL         9      9       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000244|PDB:1BLU,
FT                                ECO:0000244|PDB:3EUN,
FT                                ECO:0000244|PDB:3EXY,
FT                                ECO:0000269|PubMed:19290553,
FT                                ECO:0000269|PubMed:8880900}.
FT   METAL        12     12       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000244|PDB:1BLU,
FT                                ECO:0000244|PDB:3EUN,
FT                                ECO:0000244|PDB:3EXY,
FT                                ECO:0000269|PubMed:19290553,
FT                                ECO:0000269|PubMed:8880900}.
FT   METAL        15     15       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000244|PDB:1BLU,
FT                                ECO:0000244|PDB:3EUN,
FT                                ECO:0000244|PDB:3EXY,
FT                                ECO:0000269|PubMed:19290553,
FT                                ECO:0000269|PubMed:8880900}.
FT   METAL        19     19       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000244|PDB:1BLU,
FT                                ECO:0000244|PDB:3EUN,
FT                                ECO:0000244|PDB:3EXY,
FT                                ECO:0000269|PubMed:19290553,
FT                                ECO:0000269|PubMed:8880900}.
FT   METAL        38     38       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000244|PDB:1BLU,
FT                                ECO:0000244|PDB:3EUN,
FT                                ECO:0000244|PDB:3EXY,
FT                                ECO:0000269|PubMed:19290553,
FT                                ECO:0000269|PubMed:8880900}.
FT   METAL        41     41       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000244|PDB:1BLU,
FT                                ECO:0000244|PDB:3EUN,
FT                                ECO:0000244|PDB:3EXY,
FT                                ECO:0000269|PubMed:19290553,
FT                                ECO:0000269|PubMed:8880900}.
FT   METAL        50     50       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000244|PDB:1BLU,
FT                                ECO:0000244|PDB:3EUN,
FT                                ECO:0000244|PDB:3EXY,
FT                                ECO:0000269|PubMed:19290553,
FT                                ECO:0000269|PubMed:8880900}.
FT   METAL        54     54       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000244|PDB:1BLU,
FT                                ECO:0000244|PDB:3EUN,
FT                                ECO:0000244|PDB:3EXY,
FT                                ECO:0000269|PubMed:19290553,
FT                                ECO:0000269|PubMed:8880900}.
FT   MUTAGEN      14     14       V->G: Increases the reduction potential
FT                                of cluster 1 by approximately 50 mV.
FT                                {ECO:0000269|PubMed:19290553}.
FT   MUTAGEN      58     58       C->A: Increases the reduction potential
FT                                of cluster 1 by approximately 50 mV.
FT                                {ECO:0000269|PubMed:19290553}.
FT   MUTAGEN      58     58       C->S: No change in the reduction
FT                                potential values of the clusters.
FT                                {ECO:0000269|PubMed:19290553}.
FT   CONFLICT      8      8       E -> Q (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     13     13       D -> N (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     16     16       E -> Q (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND        3      5       {ECO:0000244|PDB:3EUN}.
FT   HELIX        16     18       {ECO:0000244|PDB:3EUN}.
FT   STRAND       24     26       {ECO:0000244|PDB:3EUN}.
FT   STRAND       28     33       {ECO:0000244|PDB:3EUN}.
FT   HELIX        35     37       {ECO:0000244|PDB:3EUN}.
FT   TURN         40     44       {ECO:0000244|PDB:3EUN}.
FT   HELIX        49     53       {ECO:0000244|PDB:3EUN}.
FT   STRAND       59     61       {ECO:0000244|PDB:3EUN}.
FT   HELIX        63     65       {ECO:0000244|PDB:3EUN}.
FT   HELIX        69     80       {ECO:0000244|PDB:3EUN}.
SQ   SEQUENCE   83 AA;  9189 MW;  C281B9500D1B969F CRC64;
     MALMITDECI NCDVCEPECP NGAISQGDET YVIEPSLCTE CVGHYETSQC VEVCPVDCII
     KDPSHEETED ELRAKYERIT GEG
//
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