Identification
Name:Thioredoxin-2
Synonyms:
  • Trx-2
  • Protein-disulfide reductase
Gene Name:trxC
Enzyme Class:
Biological Properties
General Function:Involved in electron carrier activity
Specific Function:Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
KEGG Reactions:
1.0Protein dithiol+1.0Thumb+1.0Thumb1.0Protein disulfide+1.0Thumb+1.0Thumb+1.0Thumb
1.0Protein dithiol + 1.0NAD + 1.0NADP ↔ 1.0Protein disulfide + 1.0NADH + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
Complex Reactions:
1.0Thumb+1.0Reduced Thioredoxin1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0ADP + 1.0Reduced Thioredoxin → 1.0dADP + 1.0Water + 1.0Oxidized Thioredoxin
ReactionCard
1.0Thumb+1.0Reduced Thioredoxin1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0Guanosine diphosphate + 1.0Reduced Thioredoxin → 1.0dGDP + 1.0Water + 1.0Oxidized Thioredoxin
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1.0Thumb+1.0Reduced Thioredoxin1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0CDP + 1.0Reduced Thioredoxin → 1.0dCDP + 1.0Water + 1.0Oxidized Thioredoxin
ReactionCard
1.0Reduced Thioredoxin+1.0Thumb1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0Reduced Thioredoxin + 1.0Uridine 5'-diphosphate → 1.0dUDP + 1.0Water + 1.0Oxidized Thioredoxin
ReactionCard
1.0Thumb+1.0Reduced Thioredoxin1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0Methionine sulfoxide + 1.0Reduced Thioredoxin → 1.0Water + 1.0L-Methionine + 1.0Oxidized Thioredoxin
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1.0Thumb+1.0Reduced Thioredoxin2.0Thumb+1.0Oxidized Thioredoxin
1.0Hydrogen peroxide + 1.0Reduced Thioredoxin → 2.0Water + 1.0Oxidized Thioredoxin
ReactionCard
1.0Thumb+1.0Reduced Thioredoxin2.0Thumb+1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0Phosphoadenosine phosphosulfate + 1.0Reduced Thioredoxin → 2.0Hydrogen ion + 1.0Adenosine 3',5'-diphosphate + 1.0Sulfite + 1.0Oxidized Thioredoxin
ReactionCard
1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin1.0Thumb+1.0Reduced Thioredoxin
1.0Hydrogen ion + 1.0NADPH + 1.0Oxidized Thioredoxin → 1.0NADP + 1.0Reduced Thioredoxin
ReactionCard
1.0fused thiol:disulfide interchange protein (oxidized)+1.0Reduced Thioredoxin1.0fused thiol:disulfide interchange protein (reduced)+1.0Oxidized Thioredoxin
1.0fused thiol:disulfide interchange protein (oxidized) + 1.0Reduced Thioredoxin → 1.0fused thiol:disulfide interchange protein (reduced) + 1.0Oxidized Thioredoxin
ReactionCard
1.0Protein dithiol+1.0NAD(P)(+)1.0protein disulfide+1.0NAD(P)H
1.0Protein dithiol + 1.0NAD(P)(+) → 1.0protein disulfide + 1.0NAD(P)H
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00061Adenosine 3',5'-diphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01546CDPMetaboCard
ECMDB21326dADPMetaboCard
ECMDB01245dCDPMetaboCard
ECMDB00960dGDPMetaboCard
ECMDB01000dUDPMetaboCard
ECMDB01201Guanosine diphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21232Hydrogen peroxideMetaboCard
ECMDB00696L-MethionineMetaboCard
ECMDB02005Methionine sulfoxideMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB01134Phosphoadenosine phosphosulfateMetaboCard
ECMDB00240SulfiteMetaboCard
ECMDB00295Uridine 5'-diphosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
disulfide oxidoreductase activity
electron carrier activity
oxidoreductase activity
oxidoreductase activity, acting on a sulfur group of donors
protein disulfide oxidoreductase activity
Process
cell redox homeostasis
cellular homeostasis
cellular process
glycerol ether metabolic process
metabolic process
organic ether metabolic process
small molecule metabolic process
Gene Properties
Blattner:b2582
Gene OrientationClockwise
Centisome Percentage:58.55
Left Sequence End2716757
Right Sequence End2717176
Gene Sequence:
>420 bp
GTGAAACCTGCTGCTCGTCGCCGCGCTCGTGAGTGTGCCGTCCAGGCGCTCTACTCCTGG
CAGTTGTCCCAGAACGACATCGCTGATGTTGAATACCAGTTCCTGGCTGAACAGGATGTA
AAAGACGTTGACGTCCTGTACTTCCGTGAGCTGCTGGCCGGGGTGGCGACTAATACCGCA
TACCTCGACGGACTGATGAAGCCATACCTGTCCCGCCTGCTGGAAGAACTGGGACAGGTA
GAAAAAGCAGTACTGCGCATTGCGCTGTACGAACTGTCTAAACGTAGCGATGTGCCATAC
AAAGTGGCCATTAACGAAGCGATCGAACTGGCGAAATCGTTCGGCGCAGAAGACAGCCAT
AAGTTCGTCAACGGCGTACTCGATAAAGCAGCACCTGTGATTCGCCCTAACAAAAAGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:139
Protein Molecular Weight:15555
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Thioredoxin-2
MNTVCTHCQAINRIPDDRIEDAAKCGRCGHDLFDGEVINATGETLDKLLKDDLPVVIDFW
APWCGPCRNFAPIFEDVAQERSGKVRFVKVNTEAERELSSRFGIRSIPTIMIFKNGQVVD
MLNGAVPKAPFDSWLNESL
References
External Links:
ResourceLink
Uniprot ID:P0AGG4
Uniprot Name:THIO2_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674556
Ecogene ID:EG11887
Ecocyc:EG11887
ColiBase:b2582
Kegg Gene:b2582
EchoBASE ID:EB1833
CCDB:THIO2_ECOLI
BacMap:16130507
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Miranda-Vizuete, A., Damdimopoulos, A. E., Gustafsson, J., Spyrou, G. (1997). "Cloning, expression, and characterization of a novel Escherichia coli thioredoxin." J Biol Chem 272:30841-30847. Pubmed: 9388228
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837