P07591 · TRXM_SPIOL
- ProteinThioredoxin M-type, chloroplastic
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids181 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase.
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 98 | Deprotonates C-terminal active site Cys | ||||
Sequence: D | ||||||
Active site | 104 | Nucleophile | ||||
Sequence: C | ||||||
Site | 105 | Contributes to redox potential value | ||||
Sequence: G | ||||||
Site | 106 | Contributes to redox potential value | ||||
Sequence: P | ||||||
Active site | 107 | Nucleophile | ||||
Sequence: C |
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 | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | enzyme activator activity | |
Molecular Function | protein-disulfide reductase activity |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThioredoxin M-type, chloroplastic
- Short namesTrx-M
- Cleaved into 2 chains
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > Caryophyllales > Chenopodiaceae > Chenopodioideae > Anserineae > Spinacia
Accessions
- Primary accessionP07591
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 25 | |||||
Sequence: H → Y | ||||||
Natural variant | 33 | |||||
Sequence: V → L | ||||||
Natural variant | 37 | |||||
Sequence: T → S | ||||||
Mutagenesis | 107 | Prevents scission of the intermolecular disulfide bond by the second Cys of the active site. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3 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: MAIENCLQLSTSASVGTVAVKSHVHHLQPSSKVNVPTFRGLKRSFPALSSSVSSSSPRQFRYSSVVC | ||||||
Chain | PRO_0000034178 | 68-181 | Thioredoxin M-type, chloroplastic | |||
Sequence: KASEAVKEVQDVNDSSWKEFVLESEVPVMVDFWAPWCGPCKLIAPVIDELAKEYSGKIAVYKLNTDEAPGIATQYNIRSIPTVLFFKNGERKESIIGAVPKSTLTDSIEKYLSP | ||||||
Chain | PRO_0000045891 | 69-181 | Thioredoxin M-type Mc | |||
Sequence: ASEAVKEVQDVNDSSWKEFVLESEVPVMVDFWAPWCGPCKLIAPVIDELAKEYSGKIAVYKLNTDEAPGIATQYNIRSIPTVLFFKNGERKESIIGAVPKSTLTDSIEKYLSP | ||||||
Chain | PRO_0000045892 | 70-181 | Thioredoxin M-type Md | |||
Sequence: SEAVKEVQDVNDSSWKEFVLESEVPVMVDFWAPWCGPCKLIAPVIDELAKEYSGKIAVYKLNTDEAPGIATQYNIRSIPTVLFFKNGERKESIIGAVPKSTLTDSIEKYLSP | ||||||
Disulfide bond | 104↔107 | Redox-active | ||||
Sequence: CGPC |
Keywords
- PTM
Interaction
Subunit
Forms a complex with heterodimeric ferredoxin-thioredoxin reductase (FTR) and ferredoxin.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P07591 | ftrC Q55389 | 4 | EBI-537449, EBI-863211 | |
XENO | P07591 | PRXQ Q9LU86 | 2 | EBI-537449, EBI-540311 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 68-180 | Thioredoxin | ||||
Sequence: KASEAVKEVQDVNDSSWKEFVLESEVPVMVDFWAPWCGPCKLIAPVIDELAKEYSGKIAVYKLNTDEAPGIATQYNIRSIPTVLFFKNGERKESIIGAVPKSTLTDSIEKYLS |
Sequence similarities
Belongs to the thioredoxin family. Plant M-type subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length181
- Mass (Da)19,840
- Last updated1997-11-01 v2
- Checksum5127D4BDF72D81E9
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 83 | in Ref. 2; AA sequence | ||||
Sequence: S → G | ||||||
Sequence conflict | 90-95 | in Ref. 2; AA sequence | ||||
Sequence: ESEVPV → QSSEPS | ||||||
Sequence conflict | 128 | in Ref. 2; AA sequence | ||||
Sequence: Y → T | ||||||
Sequence conflict | 165-170 | in Ref. 2; AA sequence | ||||
Sequence: AVPKST → DVSKYQ |
Keywords
- Technical term