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Protein

Ferredoxin-1, chloroplastic

Gene

PETF

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi89Iron-sulfur (2Fe-2S)1
Metal bindingi94Iron-sulfur (2Fe-2S)1
Metal bindingi97Iron-sulfur (2Fe-2S)1
Metal bindingi127Iron-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

Enzyme and pathway databases

SABIO-RKP00221.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin-1, chloroplastic
Alternative name(s):
Ferredoxin I
Short name:
Fd I
Gene namesi
Name:PETF
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 50Chloroplast1 PublicationAdd BLAST50
ChainiPRO_000000883951 – 147Ferredoxin-1, chloroplasticAdd BLAST97

Interactioni

Subunit structurei

Forms a complex with heterodimeric ferredoxin-thioredoxin reductase (FTR) and thioredoxin.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
narBP394582EBI-864933,EBI-932578From a different organism.
PETHP004553EBI-864933,EBI-865079
psaDP123532EBI-864933,EBI-864919

Protein-protein interaction databases

IntActiP00221. 4 interactors.

Structurei

Secondary structure

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi52 – 59Combined sources8
Beta strandi62 – 69Combined sources8
Helixi74 – 80Combined sources7
Beta strandi88 – 92Combined sources5
Beta strandi98 – 104Combined sources7
Helixi116 – 121Combined sources6
Beta strandi123 – 125Combined sources3
Helixi126 – 128Combined sources3
Beta strandi130 – 133Combined sources4
Beta strandi135 – 138Combined sources4
Helixi142 – 144Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A70X-ray1.70A51-147[»]
ProteinModelPortaliP00221.
SMRiP00221.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00221.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 1432Fe-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

Keywords - Domaini

Transit peptide

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.

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

P00221-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATTTTMMG MATTFVPKPQ APPMMAALPS NTGRSLFGLK TGSRGGRMTM
60 70 80 90 100
AAYKVTLVTP TGNVEFQCPD DVYILDAAEE EGIDLPYSCR AGSCSSCAGK
110 120 130 140
LKTGSLNQDD QSFLDDDQID EGWVLTCAAY PVSDVTIETH KEEELTA
Length:147
Mass (Da):15,658
Last modified:August 1, 1991 - v2
Checksum:i76045050A0AA8697
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35660 mRNA. Translation: AAA34028.1.
PIRiS00437. FESP1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35660 mRNA. Translation: AAA34028.1.
PIRiS00437. FESP1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A70X-ray1.70A51-147[»]
ProteinModelPortaliP00221.
SMRiP00221.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00221. 4 interactors.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP00221.

Miscellaneous databases

EvolutionaryTraceiP00221.

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_SPIOL
AccessioniPrimary (citable) accession number: P00221
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1991
Last modified: November 2, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

There may be variants with Lys-81 and Met-83 and a possible deletion of Lys-141.

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.