Reviewed,
UniProtKB/Swiss-Prot P00246 (FER_SPIPL)
Last modified
November 25, 2008.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Ferredoxin |
| Organism | Spirulina platensis |
| Taxonomic identifier | 118562 [NCBI] |
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriales › Arthrospira |
Protein attributes
| Sequence length | 99 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. |
| Cofactor | Binds 1 2Fe-2S cluster. |
| Sequence similarities | Belongs to the 2Fe2S plant-type ferredoxin family. Contains 1 2Fe-2S ferredoxin-type domain. |
Ontologies
Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Ligand | 2Fe-2S Iron Iron-sulfur Metal-binding |
| Technical term | 3D-structure Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: InterPro transportInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||||||||||||||||||||
| Chain | 2 – 99 | 98 | Ferredoxin | PRO_0000189371 | |||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||
| Domain | 4 – 96 | 93 | 2Fe-2S ferredoxin-type | ||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||
| Metal binding | 42 | 1 | Iron-sulfur (2Fe-2S) | ||||||||||||||||||||||||
| Metal binding | 47 | 1 | Iron-sulfur (2Fe-2S) | ||||||||||||||||||||||||
| Metal binding | 50 | 1 | Iron-sulfur (2Fe-2S) | ||||||||||||||||||||||||
| Metal binding | 80 | 1 | Iron-sulfur (2Fe-2S) | ||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||
| Beta strand | 5 – 9 | 5 | |||||||||||||||||||||||||
| Beta strand | 16 – 20 | 5 | |||||||||||||||||||||||||
| Helix | 27 – 33 | 7 | |||||||||||||||||||||||||
| Beta strand | 41 – 46 | 6 | |||||||||||||||||||||||||
| Beta strand | 48 – 60 | 13 | |||||||||||||||||||||||||
| Helix | 69 – 73 | 5 | |||||||||||||||||||||||||
| Helix | 79 – 81 | 3 | |||||||||||||||||||||||||
| Beta strand | 83 – 93 | 11 | |||||||||||||||||||||||||
| Turn | 95 – 97 | 3 | |||||||||||||||||||||||||
Sequences
References
| [1] | "The complete amino acid sequence of the Spirulina platensis ferredoxin." Tanaka M., Haniu M., Yasunobu K.T., Rao K.K., Hall D.O. Biochem. Biophys. Res. Commun. 69:759-765(1976) [PubMed: 817723] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-99. |
| [2] | "X-ray analysis of a [2Fe-2S] ferrodoxin from Spirulina platensis. Main chain fold and location of side chains at 2.5-A resolution." Tsukihara T., Fukuyama K., Nakamura M., Katsube Y., Tanaka N., Kakudo M., Wada K., Hase T., Matsubara H. J. Biochem. 90:1763-1773(1981) [PubMed: 6801028] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). |
| [3] | "Structure of S. platensis [2Fe-2S] ferredoxin and evolution of chloroplast-type ferrodoxins." Fukuyama K., Hase T., Matsumoto S., Tsukihara T., Katsube Y., Tanaka N., Kakudo M., Wada K., Hase T., Matsubara H. Nature 286:522-524(1980) Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | FESGAL. A00250. | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR006058. 2Fe2S_fd_BS. IPR012675. b-grasp_ferredoxin-like. IPR010241. Fdx_pln. IPR001041. Ferredoxin. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. | ||||||||||||
| Pfam | PF00111. Fer2. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR02008. fdx_plant. 1 hit. | ||||||||||||
| PROSITE | PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| LinkHub | P00246. | ||||||||||||
Entry information
| Entry name | FER_SPIPL | ||||||||
| Accession | Primary (citable) accession number: P00246 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


