O22229 · TRXB3_ARATH
- ProteinNADPH-dependent thioredoxin reductase 3
- GeneNTRC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids529 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- [thioredoxin]-dithiol + NADP+ = [thioredoxin]-disulfide + H+ + NADPH
RHEA-COMP:10698 CHEBI:29950 Position: nCHEBI:29950 Position: n+3+ CHEBI:58349 = RHEA-COMP:10700 CHEBI:50058 Position: n/n+3+ CHEBI:15378 + CHEBI:57783
Cofactor
Note: Binds 1 FAD per subunit.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 91-94 | FAD (UniProtKB | ChEBI) | ||||
Sequence: SGPA | ||||||
Binding site | 113-120 | FAD (UniProtKB | ChEBI) | ||||
Sequence: EGYQMGGV | ||||||
Binding site | 133 | FAD (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 166 | FAD (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 220 | FAD (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 240 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Site | 241 | Important for activity | ||||
Sequence: A | ||||||
Site | 259 | Important for activity | ||||
Sequence: V | ||||||
Site | 260 | Important for activity | ||||
Sequence: R | ||||||
Binding site | 265 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 324 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 344 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 364 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 371 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 371-374 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RQAV | ||||||
Active site | 454 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 457 | Nucleophile | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast stroma | |
Cellular Component | cytosol | |
Molecular Function | enzyme activator activity | |
Molecular Function | oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor | |
Molecular Function | thioredoxin-disulfide reductase (NADPH) activity | |
Biological Process | cell redox homeostasis | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | positive regulation of catalytic activity | |
Biological Process | regulation of chlorophyll biosynthetic process | |
Biological Process | regulation of starch biosynthetic process | |
Biological Process | removal of superoxide radicals |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADPH-dependent thioredoxin reductase 3
- EC number
- Short namesNTR3
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO22229
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
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.
PTM/Processing
Features
Showing features for transit peptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-67 | Chloroplast | ||||
Sequence: MAASPKIGIGIASVSSPHRVSAASSALSPPPHLFFLTTTTTTRHGGSYLLRQPTRTRSSDSLRLRVS | ||||||
Chain | PRO_0000394552 | 68-529 | NADPH-dependent thioredoxin reductase 3 | |||
Sequence: ATANSPSSSSSGGEIIENVVIIGSGPAGYTAAIYAARANLKPVVFEGYQMGGVPGGQLMTTTEVENFPGFPDGITGPDLMEKMRKQAERWGAELYPEDVESLSVTTAPFTVQTSERKVKCHSIIYATGATARRLRLPREEEFWSRGISACAICDGASPLFKGQVLAVVGGGDTATEEALYLTKYARHVHLLVRRDQLRASKAMQDRVINNPNITVHYNTETVDVLSNTKGQMSGILLRRLDTGEETELEAKGLFYGIGHSPNSQLLEGQVELDSSGYVLVREGTSNTSVEGVFAAGDVQDHEWRQAVTAAGSGCIAALSAERYLTSNNLLVEFHQPQTEEAKKEFTQRDVQEKFDITLTKHKGQYALRKLYHESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGVKMKKEYREFIEANK | ||||||
Disulfide bond | 217↔220 | Redox-active | ||||
Sequence: CAIC | ||||||
Disulfide bond | 454↔457 | Redox-active | ||||
Sequence: CGPC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
May homodimerize. Interacts with the 2-Cys peroxiredoxin BAS1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O22229 | VAL2 Q5CCK4 | 3 | EBI-4427818, EBI-15193683 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 54-78 | Disordered | ||||
Sequence: TRTRSSDSLRLRVSATANSPSSSSS | ||||||
Domain | 403-529 | Thioredoxin | ||||
Sequence: PQTEEAKKEFTQRDVQEKFDITLTKHKGQYALRKLYHESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGVKMKKEYREFIEANK |
Sequence similarities
Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length529
- Mass (Da)57,950
- Last updated2002-06-01 v2
- Checksum53853134652D64AA
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 399 | in Ref. 3; AAN18085/AAL08250 | ||||
Sequence: E → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |