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Protein

Ferredoxin-1

Gene
N/A
Organism
Equisetum arvense (Field horsetail) (Common horsetail)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi38Iron-sulfur (2Fe-2S)1
Metal bindingi43Iron-sulfur (2Fe-2S)1
Metal bindingi46Iron-sulfur (2Fe-2S)1
Metal bindingi76Iron-sulfur (2Fe-2S)1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin-1
Alternative name(s):
Ferredoxin I
OrganismiEquisetum arvense (Field horsetail) (Common horsetail)
Taxonomic identifieri3258 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaMoniliformopsesEquisetidaeEquisetalesEquisetaceaeEquisetum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001893281 – 95Ferredoxin-1Add BLAST95

Structurei

Secondary structure

195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Beta strandi11 – 17Combined sources7
Helixi23 – 29Combined sources7
Beta strandi37 – 44Combined sources8
Beta strandi47 – 53Combined sources7
Helixi65 – 69Combined sources5
Beta strandi72 – 74Combined sources3
Turni75 – 77Combined sources3
Beta strandi79 – 82Combined sources4
Beta strandi84 – 87Combined sources4
Turni91 – 94Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FRRX-ray1.80A/B1-95[»]
ProteinModelPortaliP00235.
SMRiP00235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00235.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST91

Sequence similaritiesi

Belongs to the 2Fe2S plant-type ferredoxin family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR010241. Fd_pln.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR02008. fdx_plant. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00235-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AYKTVLKTPS GEFTLDVPEG TTILDAAEEA GYDLPFSCRA GACSSCLGKV
60 70 80 90
VSGSVDESEG SFLDDGQMEE GFVLTCIAIP ESDLVIETHK EEELF
Length:95
Mass (Da):10,098
Last modified:July 21, 1986 - v1
Checksum:i3AB5F5F3E72C44E2
GO

Sequence databases

PIRiA04609. FEEQ1F.

Cross-referencesi

Sequence databases

PIRiA04609. FEEQ1F.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FRRX-ray1.80A/B1-95[»]
ProteinModelPortaliP00235.
SMRiP00235.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00235.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR010241. Fd_pln.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR02008. fdx_plant. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFER1_EQUAR
AccessioniPrimary (citable) accession number: P00235
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.