Glutaredoxin-3 (P0AC62)

Identification
Name:Glutaredoxin-3
Synonyms:
  • Grx3
Gene Name:grxC
Enzyme Class:Not Available
Biological Properties
General Function:Involved in electron carrier activity
Specific Function:The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Complex Reactions:
1.0glutaredoxin+1.0Thumb → 1.0Thumb+1.0glutaredoxin+1.0Thumb
1.0glutaredoxin + 1.0Uridine 5'-diphosphate → 1.0dUDP + 1.0glutaredoxin + 1.0Water
ReactionCard
1.0Thumb+1.0glutaredoxin → 1.0Thumb+1.0glutaredoxin+1.0Thumb
1.0Guanosine diphosphate + 1.0glutaredoxin → 1.0dGDP + 1.0glutaredoxin + 1.0Water
ReactionCard
1.0Thumb+1.0glutaredoxin → 1.0Thumb+1.0glutaredoxin+1.0Thumb
1.0CDP + 1.0glutaredoxin → 1.0dCDP + 1.0glutaredoxin + 1.0Water
ReactionCard
1.0Thumb+1.0glutaredoxin → 1.0Thumb+1.0glutaredoxin+1.0Thumb
1.0ADP + 1.0glutaredoxin → 1.0dADP + 1.0glutaredoxin + 1.0Water
ReactionCard
1.0glutaredoxin+1.0Thumb → 1.0glutaredoxin+2.0Thumb+1.0Thumb+1.0Thumb
1.0glutaredoxin + 1.0Phosphoadenosine phosphosulfate → 1.0glutaredoxin + 2.0Hydrogen ion + 1.0Adenosine 3',5'-diphosphate + 1.0Sulfite
ReactionCard
1.0glutaredoxin+2.0Thumb → 1.0glutaredoxin+1.0Thumb
1.0glutaredoxin + 2.0Glutathione → 1.0glutaredoxin + 1.0Glutathione disulfide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00061Adenosine 3',5'-diphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01546CDPMetaboCard
ECMDB21326dADPMetaboCard
ECMDB01245dCDPMetaboCard
ECMDB00960dGDPMetaboCard
ECMDB01000dUDPMetaboCard
ECMDB00125GlutathioneMetaboCard
ECMDB21221Glutathione disulfideMetaboCard
ECMDB01201Guanosine diphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
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
Gene Properties
Blattner:b3610
Gene OrientationCounterclockwise
Centisome Percentage:81.52
Left Sequence End3782214
Right Sequence End3782465
Gene Sequence:
>252 bp
ATGGCCAATGTTGAAATCTATACCAAAGAAACCTGCCCGTATTGCCATCGTGCAAAAGCA
CTGCTGAGCAGCAAGGGCGTGAGTTTCCAGGAGCTGCCGATCGATGGCAACGCCGCCAAG
CGTGAAGAGATGATCAAACGCAGCGGTCGCACCACGGTTCCCCAGATTTTTATTGACGCA
CAGCACATTGGCGGCTGTGATGACTTGTATGCATTGGATGCACGTGGTGGACTGGATCCC
CTGCTGAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:83
Protein Molecular Weight:9137
Protein Theoretical pI:7
PDB File:1FOV
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glutaredoxin-3
MANVEIYTKETCPYCHRAKALLSSKGVSFQELPIDGNAAKREEMIKRSGRTTVPQIFIDA
QHIGGCDDLYALDARGGLDPLLK
References
External Links:
ResourceLink
Uniprot ID:P0AC62
Uniprot Name:GLRX3_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676432
PDB ID:1FOV
Ecogene ID:EG12294
Ecocyc:EG12294
ColiBase:b3610
Kegg Gene:b3610
EchoBASE ID:EB2202
CCDB:GLRX3_ECOLI
BacMap:16131481
General Reference:
  • Aslund, F., Ehn, B., Miranda-Vizuete, A., Pueyo, C., Holmgren, A. (1994). "Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant." Proc Natl Acad Sci U S A 91:9813-9817. Pubmed: 7937896
  • Aslund, F., Nordstrand, K., Berndt, K. D., Nikkola, M., Bergman, T., Ponstingl, H., Jornvall, H., Otting, G., Holmgren, A. (1996). "Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis." J Biol Chem 271:6736-6745. Pubmed: 8636094
  • 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
  • Nordstrand, K., Sandstrom, A., Aslund, F., Holmgren, A., Otting, G., Berndt, K. D. (2000). "NMR structure of oxidized glutaredoxin 3 from Escherichia coli." J Mol Biol 303:423-432. Pubmed: 11031118
  • Nordstrand, K., slund, F., Holmgren, A., Otting, G., Berndt, K. D. (1999). "NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism." J Mol Biol 286:541-552. Pubmed: 9973569
  • Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G. 3rd, Blattner, F. R. (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 22:2576-2586. Pubmed: 8041620