O22229 · TRXB3_ARATH

Function

function

Thioredoxin reductase (TR) that exhibits both TR and thioredoxin (Trx) activities. Contains a C-terminal functional Trx domain. Functions as an electron donor for plastidial 2-Cys peroxiredoxins and participates in a NADPH-dependent hydrogen peroxide scavenging system in chloroplasts in the dark. Required for chlorophyll biosynthesis and biogenesis of the photosynthetic apparatus. Activates aerobic cyclase which converts Mg-protoporhyrin monomethyl ester into protochlorophyllide. Involved in a light-dependent regulation of starch biosynthesis by redox activation of the ADP-glucose pyrophosphorylase (AGPase), a central enzyme of starch synthesis.

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.

Features

Showing features for binding site, site, active site.

TypeIDPosition(s)Description
Binding site91-94FAD (UniProtKB | ChEBI)
Binding site113-120FAD (UniProtKB | ChEBI)
Binding site133FAD (UniProtKB | ChEBI)
Binding site166FAD (UniProtKB | ChEBI)
Binding site220FAD (UniProtKB | ChEBI)
Binding site240NADP+ (UniProtKB | ChEBI)
Site241Important for activity
Site259Important for activity
Site260Important for activity
Binding site265NADP+ (UniProtKB | ChEBI)
Binding site324NADP+ (UniProtKB | ChEBI)
Binding site344NADP+ (UniProtKB | ChEBI)
Binding site364FAD (UniProtKB | ChEBI)
Binding site371NADP+ (UniProtKB | ChEBI)
Binding site371-374FAD (UniProtKB | ChEBI)
Active site454Nucleophile
Active site457Nucleophile

GO annotations

AspectTerm
Cellular Componentchloroplast
Cellular Componentchloroplast stroma
Cellular Componentcytosol
Molecular Functionenzyme activator activity
Molecular Functionoxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
Molecular Functionthioredoxin-disulfide reductase (NADPH) activity
Biological Processcell redox homeostasis
Biological Processhydrogen peroxide catabolic process
Biological Processpositive regulation of catalytic activity
Biological Processregulation of chlorophyll biosynthetic process
Biological Processregulation of starch biosynthetic process
Biological Processremoval of superoxide radicals

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NADPH-dependent thioredoxin reductase 3
  • EC number
  • Short names
    NTR3
  • Alternative names
    • NADPH-dependent thioredoxin reductase C
      (ANTR-C
      ; AtNTRC
      )

Gene names

    • Name
      NTRC
    • ORF names
      T32G6.20
    • Ordered locus names
      At2g41680

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    O22229
  • Secondary accessions
    • Q0WM62
    • Q93ZQ1

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Dwarf plants with chlorotic leaves. Accumulation of Mg-protoporhyrin after feeding with 5-aminolevulinic acid.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 14 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for transit peptide, chain, disulfide bond.

TypeIDPosition(s)Description
Transit peptide1-67Chloroplast
ChainPRO_000039455268-529NADPH-dependent thioredoxin reductase 3
Disulfide bond217↔220Redox-active
Disulfide bond454↔457Redox-active

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

May homodimerize. Interacts with the 2-Cys peroxiredoxin BAS1.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY O22229VAL2 Q5CCK43EBI-4427818, EBI-15193683

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region54-78Disordered
Domain403-529Thioredoxin

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    529
  • Mass (Da)
    57,950
  • Last updated
    2002-06-01 v2
  • Checksum
    53853134652D64AA
MAASPKIGIGIASVSSPHRVSAASSALSPPPHLFFLTTTTTTRHGGSYLLRQPTRTRSSDSLRLRVSATANSPSSSSSGGEIIENVVIIGSGPAGYTAAIYAARANLKPVVFEGYQMGGVPGGQLMTTTEVENFPGFPDGITGPDLMEKMRKQAERWGAELYPEDVESLSVTTAPFTVQTSERKVKCHSIIYATGATARRLRLPREEEFWSRGISACAICDGASPLFKGQVLAVVGGGDTATEEALYLTKYARHVHLLVRRDQLRASKAMQDRVINNPNITVHYNTETVDVLSNTKGQMSGILLRRLDTGEETELEAKGLFYGIGHSPNSQLLEGQVELDSSGYVLVREGTSNTSVEGVFAAGDVQDHEWRQAVTAAGSGCIAALSAERYLTSNNLLVEFHQPQTEEAKKEFTQRDVQEKFDITLTKHKGQYALRKLYHESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGVKMKKEYREFIEANK

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict399in Ref. 3; AAN18085/AAL08250

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC002510
EMBL· GenBank· DDBJ
AAB84351.2
EMBL· GenBank· DDBJ
Genomic DNA
CP002685
EMBL· GenBank· DDBJ
AEC10015.1
EMBL· GenBank· DDBJ
Genomic DNA
AY056394
EMBL· GenBank· DDBJ
AAL08250.1
EMBL· GenBank· DDBJ
mRNA
BT000516
EMBL· GenBank· DDBJ
AAN18085.1
EMBL· GenBank· DDBJ
mRNA
AK229969
EMBL· GenBank· DDBJ
BAF01794.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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