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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.
PhylomeDBiP0A9R4.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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.
PhylomeDBiP0A9R4.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A9R4.
PROiP0A9R4.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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...

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: September 7, 2016
This is version 98 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.