GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
ECOLI:THIO2
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | trxC (synonyms: yfiG) | |
| Protein Name(s) | Thioredoxin-2
Trx-2 Protein-disulfide reductase | |
| External Links | ||
| UniProt | P0AGG4 | |
| EMBL | U85942 U00096 AP009048 D13169 | |
| PIR | E65036 | |
| RefSeq | NP_417077.1 YP_490810.1 | |
| ProteinModelPortal | P0AGG4 | |
| SMR | P0AGG4 | |
| DIP | DIP-48115N | |
| IntAct | P0AGG4 | |
| MINT | MINT-1227521 | |
| STRING | 511145.b2582 | |
| PaxDb | P0AGG4 | |
| PRIDE | P0AGG4 | |
| EnsemblBacteria | AAC75635 BAA16469 | |
| GeneID | 12934426 947062 | |
| KEGG | ecj:Y75_p2535 eco:b2582 | |
| PATRIC | 32120565 | |
| EchoBASE | EB1833 | |
| EcoGene | EG11887 | |
| eggNOG | COG0526 | |
| HOGENOM | HOG000292979 | |
| InParanoid | P0AGG4 | |
| KO | K03672 | |
| OMA | MPKAPFE | |
| OrthoDB | EOG6QG8RK | |
| PhylomeDB | P0AGG4 | |
| BioCyc | EcoCyc:RED-THIOREDOXIN2-MONOMER ECOL316407:JW2566-MONOMER MetaCyc:RED-THIOREDOXIN2-MONOMER | |
| PRO | PR:P0AGG4 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P0AGG4 | |
| GO | GO:0005737 GO:0015035 GO:0047134 GO:0008270 GO:0045454 GO:0006662 | |
| Gene3D | 3.40.30.10 | |
| InterPro | IPR005746 IPR012336 IPR017937 IPR013766 | |
| PANTHER | PTHR10438 | |
| Pfam | PF00085 | |
| PIRSF | PIRSF000077 | |
| SUPFAM | SSF52833 | |
| TIGRFAMs | TIGR01068 | |
| PROSITE | PS00194 PS51352 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0047134 |
protein-disulfide reductase activity |
ECO:0000315 |
F |
Fig 1 |
complete | |||||
|
enables |
GO:0047134 |
protein-disulfide reductase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0047134 |
protein-disulfide reductase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11887 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0045454 |
cell redox homeostasis |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11031 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0016671 |
oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000047179 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0015035 |
protein disulfide oxidoreductase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11031 |
F |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11887 |
C |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11887 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0015035 |
protein disulfide oxidoreductase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006662 |
glycerol ether metabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0015035 |
protein disulfide oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0045454 |
cell redox homeostasis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0047134 |
protein-disulfide reductase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Ritz, D et al. (2000) Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli. J. Biol. Chem. 275 2505-12 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 2.4 2.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 3.0 3.1 Stewart, EJ et al. (1998) Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. EMBO J. 17 5543-50 PubMed GONUTS page
- ↑ Collet, JF et al. (2003) Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. J. Biol. Chem. 278 45325-32 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
- ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
b
o
p
