Reviewed,
UniProtKB/Swiss-Prot P00244 (FER1_APHFL)
Last modified
July 22, 2008.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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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-1 Alternative name(s): Ferredoxin I |
| Organism | Aphanizomenon flos-aquae |
| Taxonomic identifier | 1176 [NCBI] |
| Taxonomic lineage | Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Aphanizomenon |
Protein attributes
| Sequence length | 98 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 | Direct protein sequencing |
Gene Ontology (GO) | |
| None. [Check GOA] | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | ||||
Molecule processing | ||||||||
|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | |||||
| Chain | 2 – 98 | 97 | Ferredoxin-1 | |||||
Regions | ||||||||
| Domain | 4 – 95 | 92 | 2Fe-2S ferredoxin-type | |||||
Sites | ||||||||
| Metal binding | 41 | 1 | Iron-sulfur (2Fe-2S) By similarity | |||||
| Metal binding | 46 | 1 | Iron-sulfur (2Fe-2S) By similarity | |||||
| Metal binding | 49 | 1 | Iron-sulfur (2Fe-2S) By similarity | |||||
| Metal binding | 79 | 1 | Iron-sulfur (2Fe-2S) By similarity | |||||
Sequences
References
| [1] | "Amino acid sequence of ferredoxin from Aphanizomenon flos-aquae." Lee I.S., Hase T., Matsubara H., Ho K.K., Krogmann D.W. Biochim. Biophys. Acta 744:53-56(1983) Cited for: PROTEIN SEQUENCE OF 2-98. |
Cross-references
Sequence databases | |
|---|---|
| PIR | FEFZ1. A00248. |
3D structure databases | |
| HSSP | HSSP built from PDB template 4FXC based on UniProtKB P00246. |
| SMR | P00244. Positions 2-98. |
| 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] |
| ProDom | P00244. [Graphical view] [Entries sharing at least one domain] |
| BLOCKS | Search... |
Other Resources | |
| ProtoNet | Search... |
Entry information
| Entry name | FER1_APHFL | ||||||||
| Accession | Primary (citable) accession number: P00244 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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