FER_ALLVD
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 03-AUG-2022, entry version 131.
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 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC 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 vinosum
RT 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; DOI=10.1093/oxfordjournals.jbchem.a131635;
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; DOI=10.1016/s0021-9258(18)77311-0;
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:0007744|PDB:1BLU}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-83 IN COMPLEX WITH IRON-SULFUR
RP (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 vinosum:
RT evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins.";
RL Protein Sci. 5:1765-1775(1996).
RN [6] {ECO:0007744|PDB:3EUN, ECO:0007744|PDB:3EXY}
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 2-83 OF MUTANTS GLY-14 AND ALA-58
RP IN COMPLEX WITH IRON-SULFUR (4FE-4S), COFACTOR, BIOPHYSICOCHEMICAL
RP 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., Kyritsis P.,
RA 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 homologous
RT Escherichia coli ferredoxin.";
RL J. Biol. Inorg. Chem. 14:783-799(2009).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions. {ECO:0000305|PubMed:2387857}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:19290553, ECO:0000269|PubMed:8765743,
CC 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 cluster 1,
CC and -467 mV for the cluster 2 (PubMed:19290553).
CC {ECO:0000269|PubMed:19290553, ECO:0000269|PubMed:2387857};
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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 AlphaFoldDB; P00208; -.
DR SMR; P00208; -.
DR STRING; 572477.Alvin_2884; -.
DR EnsemblBacteria; ADC63789; ADC63789; Alvin_2884.
DR KEGG; alv:Alvin_2884; -.
DR eggNOG; COG1145; Bacteria.
DR HOGENOM; CLU_139698_11_0_6; -.
DR OMA; DCCVPDD; -.
DR OrthoDB; 1873445at2; -.
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 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; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:893371"
FT CHAIN 2..83
FT /note="Ferredoxin"
FT /id="PRO_0000159127"
FT DOMAIN 2..29
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 31..64
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 9
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19290553,
FT ECO:0000269|PubMed:8880900, ECO:0007744|PDB:1BLU,
FT ECO:0007744|PDB:3EUN, ECO:0007744|PDB:3EXY"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19290553,
FT ECO:0000269|PubMed:8880900, ECO:0007744|PDB:1BLU,
FT ECO:0007744|PDB:3EUN, ECO:0007744|PDB:3EXY"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19290553,
FT ECO:0000269|PubMed:8880900, ECO:0007744|PDB:1BLU,
FT ECO:0007744|PDB:3EUN, ECO:0007744|PDB:3EXY"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19290553,
FT ECO:0000269|PubMed:8880900, ECO:0007744|PDB:1BLU,
FT ECO:0007744|PDB:3EUN, ECO:0007744|PDB:3EXY"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19290553,
FT ECO:0000269|PubMed:8880900, ECO:0007744|PDB:1BLU,
FT ECO:0007744|PDB:3EUN, ECO:0007744|PDB:3EXY"
FT BINDING 41
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19290553,
FT ECO:0000269|PubMed:8880900, ECO:0007744|PDB:1BLU,
FT ECO:0007744|PDB:3EUN, ECO:0007744|PDB:3EXY"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19290553,
FT ECO:0000269|PubMed:8880900, ECO:0007744|PDB:1BLU,
FT ECO:0007744|PDB:3EUN, ECO:0007744|PDB:3EXY"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19290553,
FT ECO:0000269|PubMed:8880900, ECO:0007744|PDB:1BLU,
FT ECO:0007744|PDB:3EUN, ECO:0007744|PDB:3EXY"
FT MUTAGEN 14
FT /note="V->G: Increases the reduction potential of cluster 1
FT by approximately 50 mV."
FT /evidence="ECO:0000269|PubMed:19290553"
FT MUTAGEN 58
FT /note="C->A: Increases the reduction potential of cluster 1
FT by approximately 50 mV."
FT /evidence="ECO:0000269|PubMed:19290553"
FT MUTAGEN 58
FT /note="C->S: No change in the reduction potential values of
FT the clusters."
FT /evidence="ECO:0000269|PubMed:19290553"
FT CONFLICT 8
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:3EUN"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:3EUN"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:3EUN"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:3EUN"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3EUN"
FT TURN 40..44
FT /evidence="ECO:0007829|PDB:3EUN"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:3EUN"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3EUN"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3EUN"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:3EUN"
SQ SEQUENCE 83 AA; 9189 MW; C281B9500D1B969F CRC64;
MALMITDECI NCDVCEPECP NGAISQGDET YVIEPSLCTE CVGHYETSQC VEVCPVDCII
KDPSHEETED ELRAKYERIT GEG
