A0A2K3N1E9 · A0A2K3N1E9_TRIPR
- Proteinprotein-disulfide reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids494 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- [protein]-dithiol + NAD+ = [protein]-disulfide + H+ + NADH
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Molecular Function | thioredoxin-disulfide reductase (NADPH) activity |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameprotein-disulfide reductase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > Hologalegina > IRL clade > Trifolieae > Trifolium
Accessions
- Primary accessionA0A2K3N1E9
Proteomes
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-165 | Thioredoxin | ||||
Sequence: SILSSPGTHFLLKNNADQVGIDSLKGKKIGFYFSASWCGPCQRFTPILAEVYNELSPNGDFEVVFVSADEDEEAFKNYFSKMPWLAIPFSDTETRNSLDELFHVNGIPHLALLHETGKVITEDGVDIIRDYGAEGYPFTSERVQELKDQEEE | ||||||
Domain | 319-482 | Thioredoxin | ||||
Sequence: LDEIAKAKEATQTLESVLVSGGQDFVIKNGGEKIPVSELEGKTVLLYFSAHWCPPCRAFLPKLIDAYHKIKAQDKDTLEVVFLSSDRDQDSFDEFFAGMPWLALPFGDSRKEILSRKFKVSGIPMLVAIGPSGRTVTKEARDLIGLYGADAYPFTEERIKEIEA |
Sequence similarities
Belongs to the nucleoredoxin family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length494
- Mass (Da)55,376
- Last updated2018-03-28 v1
- ChecksumE9E2B3138713BEC3
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 494 | |||||
Sequence: K |
Keywords
- Technical term