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9CAUD:A0A024AZS4
Contents
| Species (Taxon ID) | Bacillus phage Evoli. (1486658) | |
| Gene Name(s) | No Information Provided. | |
| Protein Name(s) | Thioredoxin (ECO:0000313 with EMBL:AHZ09864.1) | |
| External Links | ||
| UniProt | A0A024AZS4 | |
| EMBL | KJ489398 | |
| RefSeq | YP_009035661.1 | |
| GeneID | 19525481 | |
| KEGG | vg:19525481 | |
| Proteomes | UP000026901 | |
| InterPro | IPR012336 | |
| SUPFAM | SSF52833 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0097619 |
PTEX complex |
ECO:0000315 |
C |
Mutagenesis of T7 gene 5 and thioredoxin. |
complete | |||||
| GO:0004791 |
thioredoxin-disulfide reductase activity |
ECO:0000314 |
F |
Previous experiments had established the amino acid sequence of the N-terminal cyanogen bromide fragment of thioredoxin and the present results give the complete amino acid sequence of thioredoxin from Escherichia coli B. The molecule contains 108 residues in a single polypeptide chain with a molecular weight of 11,657 as calculated from the sequence. The functional group of the protein occurs in position 32 to 35 and consists of a disulfide bridge formed by two half-cystine residues separated by a glycine and a proline residue. No metals were found as part of the functional group. |
complete | |||||
| GO:0004748 |
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
ECO:0000314 |
F |
This paper describes that thioredoxin has many contexts it interacts in and therefore can be called the "moonlight protein". One of its functions in nearly all organisms is DNA synthesis. "Thioredoxin is a hydrogen donor for ribonucleotide reductase" |
complete | |||||
| GO:0004791 |
thioredoxin-disulfide reductase activity |
ECO:0000314 |
F |
This paper describes that thioredoxin has many contexts it interacts in and therefore can be called the "moonlight protein". One of its roles in all organisms is protein disulfide reduction. "Thioredoxin is a key player in keeping intracellular protein disulfides generally reduced." |
complete | |||||
| GO:0008379 |
thioredoxin peroxidase activity |
ECO:0000314 |
F |
This paper describes that thioredoxin has many contexts it interacts in and therefore can be called the "moonlight protein". One function that it does in many organisms is the reduction of hydrogen peroxide. "oxidative stress and apoptosis induction, require reduction by thioredoxin" |
complete | |||||
| GO:0033745 |
L-methionine-(R)-S-oxide reductase activity |
ECO:0000314 |
F |
This paper describes that thioredoxin has many contexts it interacts in and therefore can be called the "moonlight protein". One function it does in many organisms is repairing proteins. "Thioredoxin is hydrogen donor for methionine sulfoxide reductases". |
complete | |||||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Tran, NQ et al. (2012) Thioredoxin, the processivity factor, sequesters an exposed cysteine in the thumb domain of bacteriophage T7 DNA polymerase. J. Biol. Chem. 287 39732-41 PubMed GONUTS page
- ↑ Holmgren, A (1968) Thioredoxin. 6. The amino acid sequence of the protein from escherichia coli B. Eur. J. Biochem. 6 475-84 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 3.3 Arnér, ES & Holmgren, A (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267 6102-9 PubMed GONUTS page
