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Protein

2Fe-2S ferredoxin

Gene

fdx

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins.

Cofactori

[2Fe-2S] clusterNote: Binds 1 [2Fe-2S] cluster.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi42 – 421Iron-sulfur (2Fe-2S)
Metal bindingi48 – 481Iron-sulfur (2Fe-2S)
Metal bindingi51 – 511Iron-sulfur (2Fe-2S)
Metal bindingi87 – 871Iron-sulfur (2Fe-2S)

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: EcoCyc
  • electron carrier activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • iron-sulfur cluster assembly Source: EcoCyc
  • oxidation-reduction process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:FERREDOXIN-MONOMER.
ECOL316407:JW2509-MONOMER.
MetaCyc:FERREDOXIN-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
2Fe-2S ferredoxin
Gene namesi
Name:fdx
Ordered Locus Names:b2525, JW2509
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11328. fdx.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 1111102Fe-2S ferredoxinPRO_0000201168Add
BLAST

Proteomic databases

EPDiP0A9R4.
PaxDbiP0A9R4.
PRIDEiP0A9R4.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
iscAP0AAC84EBI-767037,EBI-767026

Protein-protein interaction databases

BioGridi4260584. 40 interactions.
DIPiDIP-48512N.
IntActiP0A9R4. 13 interactions.
STRINGi511145.b2525.

Structurei

Secondary structure

1
111
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Turni10 – 123Combined sources
Beta strandi17 – 204Combined sources
Helixi27 – 337Combined sources
Beta strandi43 – 464Combined sources
Beta strandi52 – 576Combined sources
Helixi59 – 613Combined sources
Helixi67 – 737Combined sources
Beta strandi83 – 853Combined sources
Turni86 – 883Combined sources
Beta strandi96 – 994Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I7HX-ray1.70A/B/C1-111[»]
ProteinModelPortaliP0A9R4.
SMRiP0A9R4. Positions 2-110.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9R4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 1041032Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adrenodoxin/putidaredoxin family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108ZIT. Bacteria.
COG0633. LUCA.
HOGENOMiHOG000244519.
InParanoidiP0A9R4.
KOiK04755.
OMAiSACGGVC.
OrthoDBiEOG6KMB9X.
PhylomeDBiP0A9R4.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
IPR011536. Fdx_isc.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR02007. fdx_isc. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A9R4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKIVILPHQ DLCPDGAVLE ANSGETILDA ALRNGIEIEH ACEKSCACTT
60 70 80 90 100
CHCIVREGFD SLPESSEQED DMLDKAWGLE PESRLSCQAR VTDEDLVVEI
110
PRYTINHARE H
Length:111
Mass (Da):12,331
Last modified:January 23, 2007 - v2
Checksum:iF7B3240F950DC0E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81P → Y AA sequence (PubMed:4375562).Curated
Sequence conflicti63 – 631P → Q in U01827 (PubMed:8300516).Curated
Sequence conflicti68 – 692QE → HQ in U01827 (PubMed:8300516).Curated
Sequence conflicti74 – 741D → N in U01827 (PubMed:8300516).Curated
Sequence conflicti77 – 771W → R in U01827 (PubMed:8300516).Curated
Sequence conflicti91 – 933VTD → SYH in U01827 (PubMed:8300516).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88654 Genomic DNA. Translation: AAA23755.1.
U05338 Genomic DNA. Translation: AAD13474.1.
U01827 Unassigned DNA. No translation available.
U00096 Genomic DNA. Translation: AAC75578.1.
AP009048 Genomic DNA. Translation: BAA16415.1.
PIRiJC1110.
RefSeqiNP_417020.1. NC_000913.3.
WP_001124469.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75578; AAC75578; b2525.
BAA16415; BAA16415; BAA16415.
GeneIDi947160.
KEGGiecj:JW2509.
eco:b2525.
PATRICi32120445. VBIEscCol129921_2625.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88654 Genomic DNA. Translation: AAA23755.1.
U05338 Genomic DNA. Translation: AAD13474.1.
U01827 Unassigned DNA. No translation available.
U00096 Genomic DNA. Translation: AAC75578.1.
AP009048 Genomic DNA. Translation: BAA16415.1.
PIRiJC1110.
RefSeqiNP_417020.1. NC_000913.3.
WP_001124469.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I7HX-ray1.70A/B/C1-111[»]
ProteinModelPortaliP0A9R4.
SMRiP0A9R4. Positions 2-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260584. 40 interactions.
DIPiDIP-48512N.
IntActiP0A9R4. 13 interactions.
STRINGi511145.b2525.

Proteomic databases

EPDiP0A9R4.
PaxDbiP0A9R4.
PRIDEiP0A9R4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75578; AAC75578; b2525.
BAA16415; BAA16415; BAA16415.
GeneIDi947160.
KEGGiecj:JW2509.
eco:b2525.
PATRICi32120445. VBIEscCol129921_2625.

Organism-specific databases

EchoBASEiEB1304.
EcoGeneiEG11328. fdx.

Phylogenomic databases

eggNOGiENOG4108ZIT. Bacteria.
COG0633. LUCA.
HOGENOMiHOG000244519.
InParanoidiP0A9R4.
KOiK04755.
OMAiSACGGVC.
OrthoDBiEOG6KMB9X.
PhylomeDBiP0A9R4.

Enzyme and pathway databases

BioCyciEcoCyc:FERREDOXIN-MONOMER.
ECOL316407:JW2509-MONOMER.
MetaCyc:FERREDOXIN-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A9R4.
PROiP0A9R4.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
IPR011536. Fdx_isc.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR02007. fdx_isc. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from Escherichia coli."
    Ta D.T., Vickery L.E.
    J. Biol. Chem. 267:11120-11125(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11.
    Strain: K12.
  2. "Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and bgl activation, but not proU derepression, in hns-1 mutant Escherichia coli."
    Kawula T.H., Lelivelt M.J.
    J. Bacteriol. 176:610-619(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Escherichia coli ferredoxin, an iron-sulfur protein of the adrenodoxin type."
    Knoell H.-E., Knappe J.
    Eur. J. Biochem. 50:245-252(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-8.
  7. "Hyperproduction of recombinant ferredoxins in Escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster."
    Nakamura M., Saeki K., Takahashi Y.
    J. Biochem. 126:10-18(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENETIC CHARACTERIZATION.
  8. "Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters."
    Kakuta Y., Horio T., Takahashi Y., Fukuyama K.
    Biochemistry 40:11007-11012(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

Entry informationi

Entry nameiFER_ECOLI
AccessioniPrimary (citable) accession number: P0A9R4
Secondary accession number(s): P25528
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.