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ECOLI:TRXB
Contents
Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
Gene Name(s) | trxB | |
Protein Name(s) | Thioredoxin reductase
TRXR | |
External Links | ||
UniProt | P0A9P4 | |
EMBL | J03762 U00096 AP009048 L21749 M95935 | |
PIR | A28074 | |
RefSeq | NP_415408.1 YP_489160.1 | |
PDB | 1CL0 1F6M 1TDE 1TDF 1TRB | |
PDBsum | 1CL0 1F6M 1TDE 1TDF 1TRB | |
ProteinModelPortal | P0A9P4 | |
SMR | P0A9P4 | |
DIP | DIP-6168N | |
IntAct | P0A9P4 | |
STRING | 511145.b0888 | |
BindingDB | P0A9P4 | |
DrugBank | DB03147 | |
SWISS-2DPAGE | P0A9P4 | |
PaxDb | P0A9P4 | |
PRIDE | P0A9P4 | |
EnsemblBacteria | AAC73974 BAA35613 | |
GeneID | 12932721 949054 | |
KEGG | ecj:Y75_p0860 eco:b0888 | |
PATRIC | 32116985 | |
EchoBASE | EB1025 | |
EcoGene | EG11032 | |
eggNOG | COG0492 | |
HOGENOM | HOG000072912 | |
InParanoid | P0A9P4 | |
KO | K00384 | |
OMA | LEMNNGY | |
OrthoDB | EOG65XN2W | |
PhylomeDB | P0A9P4 | |
BioCyc | EcoCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER ECOL316407:JW0871-MONOMER MetaCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER | |
SABIO-RK | P0A9P4 | |
EvolutionaryTrace | P0A9P4 | |
PRO | PR:P0A9P4 | |
Proteomes | UP000000318 UP000000625 | |
Genevestigator | P0A9P4 | |
GO | GO:0005737 GO:0050660 GO:0004791 GO:0019430 | |
InterPro | IPR013027 IPR008255 IPR023753 IPR001327 IPR000103 IPR005982 | |
Pfam | PF00070 PF07992 | |
PRINTS | PR00368 PR00469 | |
TIGRFAMs | TIGR01292 | |
PROSITE | PS00573 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0004791 |
thioredoxin-disulfide reductase activity |
ECO:0000314 |
F |
Figure 13 shows the reducing ability of thioredoxin reductase. |
complete | |||||
enables |
GO:0004791 |
thioredoxin-disulfide reductase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0050660 |
flavin adenine dinucleotide 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 | |||
enables |
GO:0004791 |
thioredoxin-disulfide reductase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004791 |
thioredoxin-disulfide reductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0019430 |
removal of superoxide radicals |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004791 |
thioredoxin-disulfide reductase activity |
ECO:0000501 |
evidence 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 | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
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 | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 MOORE, EC et al. (1964) ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES.V. PURIFICATION AND PROPERTIES OF THIOREDOXIN REDUCTASE FROM ESCHERICHIA COLI B. J. Biol. Chem. 239 3445-52 PubMed GONUTS page
- ↑ 2.0 2.1 Prongay, AJ et al. (1989) Characterization of two active site mutations of thioredoxin reductase from Escherichia coli. J. Biol. Chem. 264 2656-64 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
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