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Protein

Thioredoxin-2

Gene

trxC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin.

Catalytic activityi

Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri5 – 1814Sequence analysisAdd
BLAST

GO - Molecular functioni

  • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: GO_Central
  • protein disulfide oxidoreductase activity Source: EcoCyc
  • protein-disulfide reductase activity Source: CACAO
  • zinc ion binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:RED-THIOREDOXIN2-MONOMER.
ECOL316407:JW2566-MONOMER.
MetaCyc:RED-THIOREDOXIN2-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-2 (EC:1.8.1.8)
Short name:
Trx-2
Alternative name(s):
Protein-disulfide reductase
Gene namesi
Name:trxC
Synonyms:yfiG
Ordered Locus Names:b2582, JW2566
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11887. trxC.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 139139Thioredoxin-2PRO_0000120102Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi64 ↔ 67Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP0AGG4.
PaxDbiP0AGG4.
PRIDEiP0AGG4.

Interactioni

Protein-protein interaction databases

BioGridi4263420. 8 interactions.
DIPiDIP-48115N.
IntActiP0AGG4. 25 interactions.
MINTiMINT-1227521.
STRINGi511145.b2582.

Structurei

3D structure databases

ProteinModelPortaliP0AGG4.
SMRiP0AGG4. Positions 1-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 139114ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri5 – 1814Sequence analysisAdd
BLAST

Keywords - Domaini

Redox-active center, Zinc-finger

Phylogenomic databases

eggNOGiENOG4105K63. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000292979.
InParanoidiP0AGG4.
KOiK03672.
OMAiQRVDMIN.
PhylomeDBiP0AGG4.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AGG4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTVCTHCQA INRIPDDRIE DAAKCGRCGH DLFDGEVINA TGETLDKLLK
60 70 80 90 100
DDLPVVIDFW APWCGPCRNF APIFEDVAQE RSGKVRFVKV NTEAERELSS
110 120 130
RFGIRSIPTI MIFKNGQVVD MLNGAVPKAP FDSWLNESL
Length:139
Mass (Da):15,555
Last modified:December 20, 2005 - v1
Checksum:i4C973F6FE55C8856
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85942 Genomic DNA. Translation: AAB88587.1.
U00096 Genomic DNA. Translation: AAC75635.1.
AP009048 Genomic DNA. Translation: BAA16469.2.
D13169 Genomic DNA. No translation available.
PIRiE65036.
RefSeqiNP_417077.1. NC_000913.3.
WP_001098726.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75635; AAC75635; b2582.
BAA16469; BAA16469; BAA16469.
GeneIDi947062.
KEGGiecj:JW2566.
eco:b2582.
PATRICi32120565. VBIEscCol129921_2685.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85942 Genomic DNA. Translation: AAB88587.1.
U00096 Genomic DNA. Translation: AAC75635.1.
AP009048 Genomic DNA. Translation: BAA16469.2.
D13169 Genomic DNA. No translation available.
PIRiE65036.
RefSeqiNP_417077.1. NC_000913.3.
WP_001098726.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AGG4.
SMRiP0AGG4. Positions 1-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263420. 8 interactions.
DIPiDIP-48115N.
IntActiP0AGG4. 25 interactions.
MINTiMINT-1227521.
STRINGi511145.b2582.

Proteomic databases

EPDiP0AGG4.
PaxDbiP0AGG4.
PRIDEiP0AGG4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75635; AAC75635; b2582.
BAA16469; BAA16469; BAA16469.
GeneIDi947062.
KEGGiecj:JW2566.
eco:b2582.
PATRICi32120565. VBIEscCol129921_2685.

Organism-specific databases

EchoBASEiEB1833.
EcoGeneiEG11887. trxC.

Phylogenomic databases

eggNOGiENOG4105K63. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000292979.
InParanoidiP0AGG4.
KOiK03672.
OMAiQRVDMIN.
PhylomeDBiP0AGG4.

Enzyme and pathway databases

BioCyciEcoCyc:RED-THIOREDOXIN2-MONOMER.
ECOL316407:JW2566-MONOMER.
MetaCyc:RED-THIOREDOXIN2-MONOMER.

Miscellaneous databases

PROiP0AGG4.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHIO2_ECOLI
AccessioniPrimary (citable) accession number: P0AGG4
Secondary accession number(s): P33636
, P76593, P77000, P77001
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: September 7, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.