YFHL_ECOLI
ID YFHL_ECOLI Reviewed; 86 AA.
AC P52102; Q2MAG8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ferredoxin YfhL {ECO:0000305};
DE AltName: Full=EcFd {ECO:0000303|PubMed:19290553};
GN Name=yfhL; OrderedLocusNames=b2562, JW2546;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3] {ECO:0007744|PDB:2ZVS}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-86 IN COMPLEX WITH IRON-SULFUR
RP (4FE-4S), COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
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}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:19290553};
CC Note=Binds 2 [4Fe-4S] cluster. {ECO:0000269|PubMed:19290553};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -675 mV for the cluster 1, and -418 mV for the cluster 2.
CC {ECO:0000269|PubMed:19290553};
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DR EMBL; U36841; AAA79824.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75615.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76738.1; -; Genomic_DNA.
DR PIR; A65034; A65034.
DR RefSeq; NP_417057.1; NC_000913.3.
DR RefSeq; WP_001196283.1; NZ_STEB01000011.1.
DR PDB; 2ZVS; X-ray; 1.65 A; A/B/C=2-86.
DR PDBsum; 2ZVS; -.
DR AlphaFoldDB; P52102; -.
DR SMR; P52102; -.
DR BioGRID; 4260595; 11.
DR BioGRID; 851370; 5.
DR IntAct; P52102; 12.
DR STRING; 511145.b2562; -.
DR PaxDb; P52102; -.
DR PRIDE; P52102; -.
DR EnsemblBacteria; AAC75615; AAC75615; b2562.
DR EnsemblBacteria; BAE76738; BAE76738; BAE76738.
DR GeneID; 66673550; -.
DR GeneID; 947031; -.
DR KEGG; ecj:JW2546; -.
DR KEGG; eco:b2562; -.
DR PATRIC; fig|1411691.4.peg.4172; -.
DR EchoBASE; EB3006; -.
DR eggNOG; COG1145; Bacteria.
DR HOGENOM; CLU_139698_11_0_6; -.
DR InParanoid; P52102; -.
DR OMA; DCCVPDD; -.
DR PhylomeDB; P52102; -.
DR BioCyc; EcoCyc:G7346-MON; -.
DR EvolutionaryTrace; P52102; -.
DR PRO; PR:P52102; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0002097; P:tRNA wobble base modification; IMP:EcoCyc.
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; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..86
FT /note="Ferredoxin YfhL"
FT /id="PRO_0000159300"
FT DOMAIN 1..29
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 31..65
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:0007744|PDB:2ZVS"
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:0007744|PDB:2ZVS"
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:0007744|PDB:2ZVS"
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:0007744|PDB:2ZVS"
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:0007744|PDB:2ZVS"
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:0007744|PDB:2ZVS"
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:0007744|PDB:2ZVS"
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:0007744|PDB:2ZVS"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2ZVS"
FT TURN 14..18
FT /evidence="ECO:0007829|PDB:2ZVS"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2ZVS"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2ZVS"
FT TURN 40..44
FT /evidence="ECO:0007829|PDB:2ZVS"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:2ZVS"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2ZVS"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:2ZVS"
SQ SEQUENCE 86 AA; 9791 MW; 202CFFA35FEA15DD CRC64;
MALLITKKCI NCDMCEPECP NEAISMGDHI YEINSDKCTE CVGHYETPTC QKVCPIPNTI
VKDPAHVETE EQLWDKFVLM HHADKI
