P09911 (FER1_PEA) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 86.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Ferredoxin-1, chloroplastic Alternative name(s): Ferredoxin I | ||||
| Gene names |
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| Organism | Pisum sativum (Garden pea) | ||||
| Taxonomic identifier | 3888 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum |
Protein attributes
| Sequence length | 149 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Ref.3 |
| Cofactor | Binds 1 2Fe-2S cluster. |
| Subcellular location | |
| Sequence similarities | Belongs to the 2Fe2S plant-type ferredoxin family. Contains 1 2Fe-2S ferredoxin-type domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Cellular component | Chloroplast Plastid |
| Domain | Transit peptide |
| Ligand | 2Fe-2S Iron Iron-sulfur Metal-binding |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activityInferred from electronic annotation. Source: InterPro metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| PETH | P10933 | 3 | EBI-931449,EBI-931306 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 52 | 52 | Chloroplast Ref.3 | ||||||
| Chain | 53 – 149 | 97 | Ferredoxin-1, chloroplastic | PRO_0000008836 | |||||
Regions | |||||||||
| Domain | 55 – 145 | 91 | 2Fe-2S ferredoxin-type | ||||||
Sites | |||||||||
| Metal binding | 91 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 96 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 99 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 129 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 59 | 1 | L → I in strain: cv. Onward. | ||||||
| Natural variant | 85 | 1 | I → L in strain: cv. Onward. | ||||||
Sequences
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References
| [1] | "Characterization of a single copy gene encoding ferredoxin I from pea." Elliott R.C., Pedersen T.J., Fristensky B.W., White M.J., Dickey L.F., Thompson W.F. Plant Cell 1:681-690(1989) [PubMed: 2535518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Alaska. |
| [2] | "A phytochrome regulated pea transcript encodes ferredoxin I." Dobres M.S., Elliott R.C., Watson J.C., Thompson W.F. Plant Mol. Biol. 8:53-59(1987) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-135. Strain: cv. Alaska. |
| [3] | "Comparative studies on the properties of two ferredoxins from Pisum sativum L." Dutton J.E., Rogers L.J., Haslett B.G., Takruri I.A.H., Gleaves J.T., Boulter D. J. Exp. Bot. 31:379-391(1980) Cited for: PROTEIN SEQUENCE OF 53-89, FUNCTION. Strain: cv. Onward. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M31713 Genomic DNA. Translation: AAA33665.1. M17107 mRNA. No translation available. |
| PIR | FEPM1. S11495. |
3D structure databases | |
| ProteinModelPortal | P09911. |
| SMR | P09911. Positions 53-147. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-384N. |
| IntAct | P09911. 1 interaction. |
| MINT | MINT-2584189. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR006058. 2Fe2S_fd_BS. IPR012675. Beta-grasp_ferredoxin-type. IPR010241. Fd_pln. IPR001041. Ferredoxin. [Graphical view] |
| Gene3D | G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. |
| Pfam | PF00111. Fer2. 1 hit. [Graphical view] |
| SUPFAM | SSF54292. Ferredoxin. 1 hit. |
| TIGRFAMs | TIGR02008. Fdx_plant. 1 hit. |
| PROSITE | PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FER1_PEA | ||||||||
| Accession | Primary (citable) accession number: P09911 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with