FER_ECOLI
ID FER_ECOLI Reviewed; 111 AA.
AC P0A9R4; P25528;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=2Fe-2S ferredoxin;
GN Name=fdx; OrderedLocusNames=b2525, JW2509;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12;
RX PubMed=1317854; DOI=10.1016/s0021-9258(19)49883-9;
RA Ta D.T., Vickery L.E.;
RT "Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from
RT Escherichia coli.";
RL J. Biol. Chem. 267:11120-11125(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8300516; DOI=10.1128/jb.176.3.610-619.1994;
RA Kawula T.H., Lelivelt M.J.;
RT "Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and
RT bgl activation, but not proU derepression, in hns-1 mutant Escherichia
RT coli.";
RL J. Bacteriol. 176:610-619(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 2-8.
RX PubMed=4375562; DOI=10.1111/j.1432-1033.1974.tb03893.x;
RA Knoell H.-E., Knappe J.;
RT "Escherichia coli ferredoxin, an iron-sulfur protein of the adrenodoxin
RT type.";
RL Eur. J. Biochem. 50:245-252(1974).
RN [7]
RP GENETIC CHARACTERIZATION.
RX PubMed=10393315; DOI=10.1093/oxfordjournals.jbchem.a022409;
RA Nakamura M., Saeki K., Takahashi Y.;
RT "Hyperproduction of recombinant ferredoxins in Escherichia coli by
RT coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene
RT cluster.";
RL J. Biochem. 126:10-18(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=11551196; DOI=10.1021/bi010544t;
RA Kakuta Y., Horio T., Takahashi Y., Fukuyama K.;
RT "Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin
RT involved in the assembly of iron-sulfur clusters.";
RL Biochemistry 40:11007-11012(2001).
CC -!- FUNCTION: Ferredoxin are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions. Although the function of this
CC ferredoxin is unknown it is probable that it has a role as a cellular
CC electron transfer protein. Involved in the in vivo assembly of the Fe-S
CC clusters in a wide variety of iron-sulfur proteins.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- INTERACTION:
CC P0A9R4; P0AAC8: iscA; NbExp=4; IntAct=EBI-767037, EBI-767026;
CC P0A9R4; P0A6B7: iscS; NbExp=2; IntAct=EBI-767037, EBI-550055;
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
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DR EMBL; M88654; AAA23755.1; -; Genomic_DNA.
DR EMBL; U05338; AAD13474.1; -; Genomic_DNA.
DR EMBL; U01827; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; U00096; AAC75578.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16415.1; -; Genomic_DNA.
DR PIR; JC1110; JC1110.
DR RefSeq; NP_417020.1; NC_000913.3.
DR RefSeq; WP_001124469.1; NZ_STEB01000011.1.
DR PDB; 1I7H; X-ray; 1.70 A; A/B/C=1-111.
DR PDBsum; 1I7H; -.
DR AlphaFoldDB; P0A9R4; -.
DR BMRB; P0A9R4; -.
DR SMR; P0A9R4; -.
DR BioGRID; 4260584; 52.
DR BioGRID; 851492; 4.
DR DIP; DIP-48512N; -.
DR IntAct; P0A9R4; 14.
DR STRING; 511145.b2525; -.
DR jPOST; P0A9R4; -.
DR PaxDb; P0A9R4; -.
DR PRIDE; P0A9R4; -.
DR EnsemblBacteria; AAC75578; AAC75578; b2525.
DR EnsemblBacteria; BAA16415; BAA16415; BAA16415.
DR GeneID; 67416909; -.
DR GeneID; 947160; -.
DR KEGG; ecj:JW2509; -.
DR KEGG; eco:b2525; -.
DR PATRIC; fig|1411691.4.peg.4209; -.
DR EchoBASE; EB1304; -.
DR eggNOG; COG0633; Bacteria.
DR HOGENOM; CLU_082632_5_2_6; -.
DR InParanoid; P0A9R4; -.
DR OMA; SACGGVC; -.
DR PhylomeDB; P0A9R4; -.
DR BioCyc; EcoCyc:FERREDOXIN-MON; -.
DR BioCyc; MetaCyc:FERREDOXIN-MON; -.
DR EvolutionaryTrace; P0A9R4; -.
DR PRO; PR:P0A9R4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:EcoCyc.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001055; Adrenodoxin.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR011536; Fdx_isc.
DR PANTHER; PTHR23426; PTHR23426; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR02007; fdx_isc; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00814; ADX; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1317854,
FT ECO:0000269|PubMed:4375562"
FT CHAIN 2..111
FT /note="2Fe-2S ferredoxin"
FT /id="PRO_0000201168"
FT DOMAIN 2..104
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT CONFLICT 8
FT /note="P -> Y (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="P -> Q (in Ref. 2; U01827)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..69
FT /note="QE -> HQ (in Ref. 2; U01827)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="D -> N (in Ref. 2; U01827)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="W -> R (in Ref. 2; U01827)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..93
FT /note="VTD -> SYH (in Ref. 2; U01827)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1I7H"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:1I7H"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1I7H"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:1I7H"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1I7H"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1I7H"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1I7H"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:1I7H"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1I7H"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1I7H"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1I7H"
SQ SEQUENCE 111 AA; 12331 MW; F7B3240F950DC0E0 CRC64;
MPKIVILPHQ DLCPDGAVLE ANSGETILDA ALRNGIEIEH ACEKSCACTT CHCIVREGFD
SLPESSEQED DMLDKAWGLE PESRLSCQAR VTDEDLVVEI PRYTINHARE H
