ID   FER1_AZOVI              Reviewed;         107 AA.
AC   P00214;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Ferredoxin-1;
DE   AltName: Full=Ferredoxin I;
DE            Short=FdI;
GN   Name=fdxA;
OS   Azotobacter vinelandii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2826477; DOI=10.1016/s0021-9258(19)57312-4;
RA   Morgan T.V., Lundell D.J., Burgess B.K.;
RT   "Azotobacter vinelandii ferredoxin I: cloning, sequencing, and mutant
RT   analysis.";
RL   J. Biol. Chem. 263:1370-1375(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=8244942; DOI=10.1128/jb.175.23.7707-7710.1993;
RA   Le O., Shen B., Iismaa S.E., Burgess B.K.;
RT   "Azotobacter vinelandii mutS: nucleotide sequence and mutant analysis.";
RL   J. Bacteriol. 175:7707-7710(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-107, AND X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
RX   PubMed=6848518; DOI=10.1016/s0021-9258(18)33285-x;
RA   Howard J.B., Lorsbach T.W., Ghosh D., Melis K., Stout C.D.;
RT   "Structure of Azotobacter vinelandii 7Fe ferredoxin. Amino acid sequence
RT   and electron density maps of residues.";
RL   J. Biol. Chem. 258:508-522(1983).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
RX   PubMed=7120409; DOI=10.1016/0022-2836(82)90451-x;
RA   Ghosh D., O'Donnell S., Furey W.F. Jr., Robbins A.H., Stout C.D.;
RT   "Iron-sulfur clusters and protein structure of Azotobacter ferredoxin at
RT   2.0-A resolution.";
RL   J. Mol. Biol. 158:73-109(1982).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
RX   PubMed=3422475; DOI=10.1073/pnas.85.4.1020;
RA   Stout G.H., Turley S., Sieker L.C., Jensen L.H.;
RT   "Structure of ferredoxin I from Azotobacter vinelandii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:1020-1022(1988).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=2926817; DOI=10.1016/0022-2836(89)90225-8;
RA   Stout G.H.;
RT   "Refinement of the 7 Fe ferredoxin from Azotobacter vinelandii at 1.9-A
RT   resolution.";
RL   J. Mol. Biol. 205:545-555(1989).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=15299532; DOI=10.1107/s0907444992007248;
RA   Merritt E.A., Stout G.H., Turley S., Sieker L.C., Jensen L.H.,
RA   Orme-Johnson W.H.;
RT   "Structure at pH 6.5 of ferredoxin I from Azotobacter vinelandii at 2.3-A
RT   resolution.";
RL   Acta Crystallogr. D 49:272-281(1993).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
RX   PubMed=9600844; DOI=10.1006/jmbi.1998.1732;
RA   Stout C.D., Stura E.A., McRee D.E.;
RT   "Structure of Azotobacter vinelandii 7Fe ferredoxin at 1.35-A resolution
RT   and determination of the [Fe-S] bonds with 0.01-A accuracy.";
RL   J. Mol. Biol. 278:629-639(1998).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX   PubMed=10387068; DOI=10.1021/bi983008i;
RA   Schipke C.G., Goodin D.B., McRee D.E., Stout C.D.;
RT   "Oxidized and reduced Azotobacter vinelandii ferredoxin I at 1.4-A
RT   resolution: conformational change of surface residues without significant
RT   change in the [3Fe-4S]+/0 cluster.";
RL   Biochemistry 38:8228-8239(1999).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   PubMed=10593945; DOI=10.1074/jbc.274.51.36479;
RA   Chen K., Tilley G.J., Sridhar V., Prasad G.S., Stout C.D., Armstrong F.A.,
RA   Burgess B.K.;
RT   "Alteration of the reduction potential of the [4Fe-4S](2+/+) cluster of
RT   Azotobacter vinelandii ferredoxin I.";
RL   J. Biol. Chem. 274:36479-36487(1999).
RN   [11]
RP   DNA-BINDING.
RX   PubMed=1855590; DOI=10.1016/0014-5793(91)80807-f;
RA   Thomson A.J.;
RT   "Does ferredoxin I (Azotobacter) represent a novel class of DNA-binding
RT   proteins that regulate gene expression in response to cellular iron(II)?";
RL   FEBS Lett. 285:230-236(1991).
RN   [12]
RP   MUTAGENESIS.
RX   PubMed=2153958; DOI=10.1073/pnas.87.2.598;
RA   Martin A.E., Burgess B.K., Stout C.D., Cash V.L., Dean D.R., Jensen G.M.,
RA   Stephens P.J.;
RT   "Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S]
RT   cluster-driven protein rearrangement.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:598-602(1990).
RN   [13]
RP   MUTAGENESIS.
RX   PubMed=1657971; DOI=10.1016/s0021-9258(18)54675-5;
RA   Iismaa S.E., Vazquez A.E., Jensen G.M., Stephens P.J., Butt J.N.,
RA   Armstrong F.A., Burgess B.K.;
RT   "Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I. Changes
RT   in [4Fe-4S] cluster reduction potential and reactivity.";
RL   J. Biol. Chem. 266:21563-21571(1991).
RN   [14]
RP   MUTAGENESIS.
RX   PubMed=8132582; DOI=10.1016/s0021-9258(17)37232-0;
RA   Shen B., Jollie D.R., Stout C.D., Diller T.C., Armstrong F.A., Gorst C.M.,
RA   la Mar G.N., Stephen P.J., Burgess B.K.;
RT   "Azotobacter vinelandii ferredoxin I. Alteration of individual surface
RT   charges and the [4FE-4S]2+/+ cluster reduction potential.";
RL   J. Biol. Chem. 269:8564-8575(1994).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions. This ferredoxin could play a
CC       role in regulating gene expression by interacting directly with DNA.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster.;
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC       Note=Binds 1 [3Fe-4S] cluster.;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is -450 mV for the 3Fe-4S, and -645 mV for the 4Fe-4S clusters.;
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DR   EMBL; J03521; AAA22125.1; -; Genomic_DNA.
DR   EMBL; M63007; AAA16869.1; -; Unassigned_DNA.
DR   PIR; A29936; FEAV.
DR   RefSeq; WP_012702380.1; NZ_FPKM01000003.1.
DR   PDB; 1A6L; X-ray; 2.10 A; A=2-107.
DR   PDB; 1AXQ; X-ray; 2.10 A; A=2-107.
DR   PDB; 1B0T; X-ray; 2.10 A; A=2-107.
DR   PDB; 1B0V; X-ray; 2.80 A; A/B/C/D=2-107.
DR   PDB; 1D3W; X-ray; 1.70 A; A=2-107.
DR   PDB; 1F5B; X-ray; 1.62 A; A=2-107.
DR   PDB; 1F5C; X-ray; 1.75 A; A=2-107.
DR   PDB; 1FD2; X-ray; 1.90 A; A=2-107.
DR   PDB; 1FDA; X-ray; 2.10 A; A=2-107.
DR   PDB; 1FDB; X-ray; 2.20 A; A=2-107.
DR   PDB; 1FDD; X-ray; 1.90 A; A=2-107.
DR   PDB; 1FER; X-ray; 2.30 A; A=2-107.
DR   PDB; 1FF2; X-ray; 2.30 A; A=2-107.
DR   PDB; 1FRH; X-ray; 2.30 A; A=2-107.
DR   PDB; 1FRI; X-ray; 2.10 A; A=2-107.
DR   PDB; 1FRJ; X-ray; 2.30 A; A=2-107.
DR   PDB; 1FRK; X-ray; 2.10 A; A=2-107.
DR   PDB; 1FRL; X-ray; 2.30 A; A=2-107.
DR   PDB; 1FRM; X-ray; 2.30 A; A=2-107.
DR   PDB; 1FRX; X-ray; 2.50 A; A=2-107.
DR   PDB; 1FTC; X-ray; 2.35 A; A/B=2-107.
DR   PDB; 1G3O; X-ray; 1.65 A; A=2-107.
DR   PDB; 1G6B; X-ray; 1.90 A; A=2-107.
DR   PDB; 1GAO; X-ray; 2.20 A; A/B/C/D=2-107.
DR   PDB; 1PC4; X-ray; 1.65 A; A=1-107.
DR   PDB; 1PC5; X-ray; 1.80 A; A=1-107.
DR   PDB; 2FD2; X-ray; 1.90 A; A=2-107.
DR   PDB; 5FD1; X-ray; 1.90 A; A=2-107.
DR   PDB; 6FD1; X-ray; 1.35 A; A=2-107.
DR   PDB; 6FDR; X-ray; 1.40 A; A=2-107.
DR   PDB; 7FD1; X-ray; 1.30 A; A=2-107.
DR   PDB; 7FDR; X-ray; 1.40 A; A=2-107.
DR   PDBsum; 1A6L; -.
DR   PDBsum; 1AXQ; -.
DR   PDBsum; 1B0T; -.
DR   PDBsum; 1B0V; -.
DR   PDBsum; 1D3W; -.
DR   PDBsum; 1F5B; -.
DR   PDBsum; 1F5C; -.
DR   PDBsum; 1FD2; -.
DR   PDBsum; 1FDA; -.
DR   PDBsum; 1FDB; -.
DR   PDBsum; 1FDD; -.
DR   PDBsum; 1FER; -.
DR   PDBsum; 1FF2; -.
DR   PDBsum; 1FRH; -.
DR   PDBsum; 1FRI; -.
DR   PDBsum; 1FRJ; -.
DR   PDBsum; 1FRK; -.
DR   PDBsum; 1FRL; -.
DR   PDBsum; 1FRM; -.
DR   PDBsum; 1FRX; -.
DR   PDBsum; 1FTC; -.
DR   PDBsum; 1G3O; -.
DR   PDBsum; 1G6B; -.
DR   PDBsum; 1GAO; -.
DR   PDBsum; 1PC4; -.
DR   PDBsum; 1PC5; -.
DR   PDBsum; 2FD2; -.
DR   PDBsum; 5FD1; -.
DR   PDBsum; 6FD1; -.
DR   PDBsum; 6FDR; -.
DR   PDBsum; 7FD1; -.
DR   PDBsum; 7FDR; -.
DR   AlphaFoldDB; P00214; -.
DR   SMR; P00214; -.
DR   OMA; DRMLYIH; -.
DR   EvolutionaryTrace; P00214; -.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.20; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR000813; 7Fe_ferredoxin.
DR   InterPro; IPR022569; Fd_C.
DR   PANTHER; PTHR42859:SF2; FERREDOXIN; 1.
DR   PANTHER; PTHR42859; OXIDOREDUCTASE; 1.
DR   Pfam; PF11953; DUF3470; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   PRINTS; PR00354; 7FE8SFRDOXIN.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; 3Fe-4S; 4Fe-4S; Direct protein sequencing; DNA-binding;
KW   Electron transport; Iron; Iron-sulfur; Metal-binding; Repeat; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6848518"
FT   CHAIN           2..107
FT                   /note="Ferredoxin-1"
FT                   /id="PRO_0000159095"
FT   DOMAIN          2..30
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          31..60
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   REGION          84..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         9
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000269|PubMed:3422475"
FT   BINDING         17
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000269|PubMed:3422475"
FT   BINDING         21
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:3422475"
FT   BINDING         40
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:3422475"
FT   BINDING         43
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:3422475"
FT   BINDING         46
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:3422475"
FT   BINDING         50
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000269|PubMed:3422475"
FT   CONFLICT        49
FT                   /note="E -> R (in Ref. 2; AAA16869)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="Q -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   TURN            10..12
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   HELIX           16..20
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:1FD2"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   TURN            37..39
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   HELIX           58..60
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   HELIX           63..66
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   HELIX           67..75
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   HELIX           92..95
FT                   /evidence="ECO:0007829|PDB:7FD1"
FT   HELIX           101..104
FT                   /evidence="ECO:0007829|PDB:7FD1"
SQ   SEQUENCE   107 AA;  12182 MW;  3B4B0D1A55765B2B CRC64;
     MAFVVTDNCI KCKYTDCVEV CPVDCFYEGP NFLVIHPDEC IDCALCEPEC PAQAIFSEDE
     VPEDMQEFIQ LNAELAEVWP NITEKKDPLP DAEDWDGVKG KLQHLER
//