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ECOLI:TRXB

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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

PMID:14245401[1]

ECO:0000314

F

Figure 13 shows the reducing ability of thioredoxin reductase.

complete
CACAO 4259

enables

GO:0004791

thioredoxin-disulfide reductase activity

PMID:14245401[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0050660

flavin adenine dinucleotide binding

PMID:2644268[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004791

thioredoxin-disulfide reductase activity

PMID:2644268[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004791

thioredoxin-disulfide reductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005982

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005982

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008255
InterPro:IPR023753

F

Seeded From UniProt

complete

involved_in

GO:0019430

removal of superoxide radicals

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005982

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005982
InterPro:IPR008255
InterPro:IPR023753

P

Seeded From UniProt

complete

enables

GO:0004791

thioredoxin-disulfide reductase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.8.1.9

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 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. 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
  3. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  4. 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