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Protein

Ferredoxin, chloroplastic

Gene

PETF

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
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 bindingi69 – 691Iron-sulfur (2Fe-2S)
Metal bindingi74 – 741Iron-sulfur (2Fe-2S)
Metal bindingi77 – 771Iron-sulfur (2Fe-2S)
Metal bindingi107 – 1071Iron-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

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin, chloroplastic
Gene namesi
Name:PETF
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

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 – 3232Chloroplast1 PublicationAdd
BLAST
Chaini33 – 12694Ferredoxin, chloroplasticPRO_0000008828Add
BLAST

Proteomic databases

PaxDbiP07839.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi3055.EDP03827.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Helixi16 – 183Combined sources
Turni19 – 224Combined sources
Beta strandi23 – 253Combined sources
Beta strandi33 – 397Combined sources
Beta strandi42 – 487Combined sources
Beta strandi50 – 523Combined sources
Helixi54 – 618Combined sources
Helixi75 – 773Combined sources
Beta strandi80 – 845Combined sources
Beta strandi86 – 905Combined sources
Helixi96 – 1016Combined sources
Beta strandi111 – 1188Combined sources
Helixi123 – 1264Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FCTNMR-A1-32[»]
2MH7NMR-A33-126[»]
2N0SNMR-B33-126[»]
ProteinModelPortaliP07839.
SMRiP07839. Positions 1-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07839.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 123912Fe-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

Phylogenomic databases

eggNOGiENOG410J0RP. Eukaryota.
COG0633. LUCA.
KOiK02639.
OMAiCTINTHQ.

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.
IPR023383. Ferredoxin_transit_pept.
[Graphical view]
PfamiPF11591. 2Fe-2S_Ferredox. 1 hit.
PF00111. 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.

P07839-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMAMRSTFA ARVGAKPAVR GARPASRMSC MAYKVTLKTP SGDKTIECPA
60 70 80 90 100
DTYILDAAEE AGLDLPYSCR AGACSSCAGK VAAGTVDQSD QSFLDDAQMG
110 120
NGFVLTCVAY PTSDCTIQTH QEEALY
Length:126
Mass (Da):13,232
Last modified:February 1, 1994 - v2
Checksum:i155AFEA9E6F6E411
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29516 Genomic DNA. Translation: AAC49171.1.
L10349 mRNA. Translation: AAA33085.1.
PIRiT08054. FEKM.
RefSeqiXP_001692808.1. XM_001692756.1.
UniGeneiCre.8738.

Genome annotation databases

EnsemblPlantsiEDP03827; EDP03827; CHLREDRAFT_147787.
GeneIDi5718285.
GrameneiEDP03827; EDP03827; CHLREDRAFT_147787.
KEGGicre:CHLREDRAFT_147787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29516 Genomic DNA. Translation: AAC49171.1.
L10349 mRNA. Translation: AAA33085.1.
PIRiT08054. FEKM.
RefSeqiXP_001692808.1. XM_001692756.1.
UniGeneiCre.8738.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FCTNMR-A1-32[»]
2MH7NMR-A33-126[»]
2N0SNMR-B33-126[»]
ProteinModelPortaliP07839.
SMRiP07839. Positions 1-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3055.EDP03827.

Proteomic databases

PaxDbiP07839.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiEDP03827; EDP03827; CHLREDRAFT_147787.
GeneIDi5718285.
GrameneiEDP03827; EDP03827; CHLREDRAFT_147787.
KEGGicre:CHLREDRAFT_147787.

Phylogenomic databases

eggNOGiENOG410J0RP. Eukaryota.
COG0633. LUCA.
KOiK02639.
OMAiCTINTHQ.

Miscellaneous databases

EvolutionaryTraceiP07839.

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.
IPR023383. Ferredoxin_transit_pept.
[Graphical view]
PfamiPF11591. 2Fe-2S_Ferredox. 1 hit.
PF00111. 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. "A cDNA clone encoding Chlamydomonas reinhardtii preferredoxin."
    Stein M., Jacquot J.-P., Miginiac-Maslow M.
    Plant Physiol. 102:1349-1350(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and sequencing of a ferredoxin gene from Chlamydomonas reinhardtii."
    Stein M., Chedozeau B., Jacquot J.-P.
    Plant Gene Register PGR95-065
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Purification, properties and complete amino acid sequence of the ferredoxin from a green alga, Chlamydomonas reinhardtii."
    Schmitter J.-M., Jacquot J.-P., Lamotte-Guery F., Beauvallet C., Dutka S., Gadal P., Decottignies P.
    Eur. J. Biochem. 172:405-412(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-126.
  4. "NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution."
    Lancelin J.-M., Bally I., Arlaud G.J., Blackledge M., Gans P., Stein M., Jacquot J.-P.
    FEBS Lett. 343:261-266(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-32.

Entry informationi

Entry nameiFER_CHLRE
AccessioniPrimary (citable) accession number: P07839
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1994
Last modified: February 17, 2016
This is version 117 of the entry and version 2 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.