A6MVV0 · A6MVV0_RHDSA

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

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster.

Features

Showing features for binding site, active site, site.

1112102030405060708090100110
TypeIDPosition(s)Description
Binding site53[4Fe-4S] cluster (UniProtKB | ChEBI)
Active site55Nucleophile
Binding site72[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site74[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site83[4Fe-4S] cluster (UniProtKB | ChEBI)
Site84Increases the nucleophilicity of the active site Cys

GO annotations

AspectTerm
Cellular Componentchloroplast
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionferredoxin-thioredoxin reductase activity
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity, acting on iron-sulfur proteins as donors

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ferredoxin-thioredoxin reductase, catalytic chain
  • EC number
  • Short names
    FTR-C
  • Alternative names
    • Ferredoxin-thioredoxin reductase subunit B

Gene names

    • Name
      ftrB

Encoded on

  • Chloroplast

Organism names

Accessions

  • Primary accession
    A6MVV0

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond55↔85Redox-active

Keywords

Interaction

Subunit

Heterodimer of subunit A (variable subunit) and subunit B (catalytic subunit). Heterodimeric FTR forms a complex with ferredoxin and thioredoxin.

Family & Domains

Sequence similarities

Belongs to the ferredoxin thioredoxin reductase beta subunit family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    112
  • Mass (Da)
    12,805
  • Last updated
    2007-07-24 v1
  • Checksum
    3B60303A67CC8421
METKLSSSLQAMRMFSETYAKKTNTFFCSDPSITAVVIEGLAKHKEEYGAPLCPCRHYDDKEAEVSSAYWNCPCVPMRERKECHCMLFLNPENEFAGGEQTIEEKLLLQNNL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EF508371
EMBL· GenBank· DDBJ
ABO70831.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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