P51386 · FTRC_PORPU
- ProteinFerredoxin-thioredoxin reductase, catalytic chain
- GeneftrB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids118 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
Catalytic activity
- [thioredoxin]-disulfide + 2 H+ + 2 reduced [2Fe-2S]-[ferredoxin] = [thioredoxin]-dithiol + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA-COMP:10700 CHEBI:50058 Position: n/n+3+ 2 CHEBI:15378 + 2 RHEA-COMP:10001 = RHEA-COMP:10698 CHEBI:29950 Position: nCHEBI:29950 Position: n+3+ 2 RHEA-COMP:10000
Cofactor
Note: Binds 1 [4Fe-4S] cluster.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 57 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 59 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 76 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 78 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 87 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 88 | Increases the nucleophilicity of the active site Cys | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | electron transfer activity | |
Molecular Function | ferredoxin-thioredoxin reductase activity | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFerredoxin-thioredoxin reductase, catalytic chain
- EC number
- Short namesFTR-C
- Alternative names
Gene names
Encoded on
- Chloroplast
Organism names
- Strain
- Taxonomic lineageEukaryota > Rhodophyta > Bangiophyceae > Bangiales > Bangiaceae > Porphyra
Accessions
- Primary accessionP51386
Subcellular Location
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000167673 | 1-118 | Ferredoxin-thioredoxin reductase, catalytic chain | |||
Sequence: MKKQNLVSFSDNLEAMRKFSETYAKRTGTFFCADNSVTAVVIEGLARHKDKYGAPLCPCRHYEDKKAEISATYWNCPCVPMRERKECHCMLFLTPDNEFTSDLQEIDKTTLLEKIASS | ||||||
Disulfide bond | 59↔89 | Redox-active | ||||
Sequence: CRHYEDKKAEISATYWNCPCVPMRERKECHC |
Keywords
- PTM
Interaction
Subunit
Heterodimer of subunit A (variable subunit) and subunit B (catalytic subunit). Heterodimeric FTR forms a complex with ferredoxin and thioredoxin (By similarity).
Structure
Sequence
- Sequence statusComplete
- Length118
- Mass (Da)13,539
- Last updated1996-10-01 v1
- ChecksumE490AE73708630A8
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U38804 EMBL· GenBank· DDBJ | AAC08272.1 EMBL· GenBank· DDBJ | Genomic DNA |