A0A3L8SDR7 · A0A3L8SDR7_CHLGU

Function

function

Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis. Also has reductase activity on hydrogen peroxide (H2O2).

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site70FAD (UniProtKB | ChEBI)
Binding site134FAD (UniProtKB | ChEBI)
Binding site199-206NAD+ (UniProtKB | ChEBI)
Binding site291NAD+ (UniProtKB | ChEBI)
Binding site333FAD (UniProtKB | ChEBI)
Active site471Proton acceptor

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrion
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionglutathione-disulfide reductase (NADPH) activity
Molecular Functionthioredoxin-disulfide reductase (NADPH) activity
Biological Processcell redox homeostasis
Biological Processcellular response to oxidative stress
Biological Processglutathione metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thioredoxin reductase 1, cytoplasmic
  • EC number
  • Alternative names
    • Peroxidase TXNRD1
    • Thioredoxin reductase TR1

Gene names

    • ORF names
      DV515_00009187

Organism names

  • Taxonomic identifier
  • Strain
    • Red01
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Passeroidea > Passeridae > Chloebia

Accessions

  • Primary accession
    A0A3L8SDR7

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond61↔66Redox-active

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain15-349FAD/NAD(P)-binding
Domain369-480Pyridine nucleotide-disulphide oxidoreductase dimerisation

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    528
  • Mass (Da)
    57,865
  • Last updated
    2019-02-13 v1
  • Checksum
    D3AE15E53F140ACC
MEVNGLTPVPGSYDYDLIVIGGGSGGLAAAKEAAKYEKKVMVLDFVTPTPQGSSWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRKFGWQFTEEVQHNWMTMTESVQNYVGSLNWGYRVALRDKKVTYENAYGEFVGPHTVKATNKKGVEKLYTAERFIIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGRTLVVGASYVALECAGFLAGLGLDVTVMVRSILLRGFDQDMANRIGEYMKEHGVKFIRQFVPIKVEEGTPGVLKVTAKSTTGDQIIEGKYNTVMLAIGRDPCTRRIGLGKVGVNINEKTGKIPVNDEEQTNVPYIYAIGDILQDKLELTPVAIQAGRLLVQRLYVGATTKCDYVNVPTTVFTPLEYGACGYSEETAVEKFGEESIEVYHSHFWPLEWTVPSRDNNKCYAKIICNIQDNERVIGFHVLGPNAGEITQGFAAAIKCGLTKEQLDSTVGIHPVCAEVFTTLSVTKRSGESIAKDSDYFYYVVLGPSVVQREQGVNSPVLWAEASCLNS

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue528

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QUSF01000028
EMBL· GenBank· DDBJ
RLW00074.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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