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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi89 – 891Iron-sulfur (2Fe-2S)
Metal bindingi94 – 941Iron-sulfur (2Fe-2S)
Metal bindingi97 – 971Iron-sulfur (2Fe-2S)
Metal bindingi127 – 1271Iron-sulfur (2Fe-2S)

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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5050Chloroplast1 PublicationAdd
BLAST
Chaini51 – 14797Ferredoxin-1, chloroplasticPRO_0000008839Add
BLAST

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 interactions.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 598Combined sources
Beta strandi62 – 698Combined sources
Helixi74 – 807Combined sources
Beta strandi88 – 925Combined sources
Beta strandi98 – 1047Combined sources
Helixi116 – 1216Combined sources
Beta strandi123 – 1253Combined sources
Helixi126 – 1283Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi135 – 1384Combined sources
Helixi142 – 1443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A70X-ray1.70A51-147[»]
ProteinModelPortaliP00221.
SMRiP00221. Positions 51-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00221.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 143912Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

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

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1A70X-ray1.70A51-147[»]
ProteinModelPortaliP00221.
SMRiP00221. Positions 51-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00221. 4 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP00221.

Miscellaneous databases

EvolutionaryTraceiP00221.

Family and domain databases

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...

Publicationsi

  1. "Analysis of cDNA clones encoding the entire ferredoxin I precursor polypeptide from spinach."
    Wedel N., Bartling D., Herrmann R.G.
    Bot. Acta 101:295-300(1988)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Spinach ferredoxin. II. Typtic, chymotryptic, and thermolytic peptides, and complete amino acid sequence."
    Matsubara H., Sasaki R.M.
    J. Biol. Chem. 243:1732-1757(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 51-147.
  3. "Structure of the mutant E92K of [2Fe-2S] ferredoxin I from Spinacia oleracea at 1.7-A resolution."
    Binda C., Coda A., Aliverti A., Zanetti G., Mattevi A.
    Acta Crystallogr. D 54:1353-1358(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT LYS-142.

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 11, 2015
This is version 102 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.