Identification
Name:Glutaredoxin-1
Synonyms:
  • Grx1
Gene Name:grxA
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+1.0Thumb1.0Thumb+1.0glutaredoxin+1.0Thumb
1.0glutaredoxin + 1.0Uridine 5'-diphosphate → 1.0dUDP + 1.0glutaredoxin + 1.0Water
ReactionCard
1.0Thumb+1.0glutaredoxin1.0Thumb+1.0glutaredoxin+1.0Thumb
1.0Guanosine diphosphate + 1.0glutaredoxin → 1.0dGDP + 1.0glutaredoxin + 1.0Water
ReactionCard
1.0Thumb+1.0glutaredoxin1.0Thumb+1.0glutaredoxin+1.0Thumb
1.0CDP + 1.0glutaredoxin → 1.0dCDP + 1.0glutaredoxin + 1.0Water
ReactionCard
1.0Thumb+1.0glutaredoxin1.0Thumb+1.0glutaredoxin+1.0Thumb
1.0ADP + 1.0glutaredoxin → 1.0dADP + 1.0glutaredoxin + 1.0Water
ReactionCard
1.0glutaredoxin+1.0Thumb1.0glutaredoxin+2.0Thumb+1.0Thumb+1.0Thumb
1.0glutaredoxin+2.0Thumb1.0glutaredoxin+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:b0849
Gene OrientationCounterclockwise
Centisome Percentage:19.18
Left Sequence End889719
Right Sequence End889976
Gene Sequence:
>258 bp
ATGCAAACCGTTATTTTTGGTCGTTCGGGTTGCCCTTACTGTGTGCGTGCAAAAGATCTG
GCTGAGAAATTGAGCAATGAACGCGATGATTTTCAGTATCAGTATGTAGATATTCGTGCG
GAAGGGATCACTAAAGAAGATCTACAACAAAAGGCAGGTAAACCCGTAGAAACCGTGCCG
CAGATTTTTGTCGATCAGCAACATATCGGCGGCTATACCGATTTTGCTGCATGGGTGAAA
GAAAATCTGGACGCCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:85
Protein Molecular Weight:9685
Protein Theoretical pI:5
PDB File:1EGR
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glutaredoxin-1
MQTVIFGRSGCPYCVRAKDLAEKLSNERDDFQYQYVDIRAEGITKEDLQQKAGKPVETVP
QIFVDQQHIGGYTDFAAWVKENLDA
References
External Links:
ResourceLink
Uniprot ID:P68688
Uniprot Name:GLRX1_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674778
PDB ID:1EGR
Ecogene ID:EG10417
Ecocyc:EG10417
ColiBase:b0849
Kegg Gene:b0849
EchoBASE ID:EB0412
CCDB:GLRX1_ECOLI
BacMap:16128817
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
  • Hoog, J. O., Jornvall, H., Holmgren, A., Carlquist, M., Persson, M. (1983). "The primary structure of Escherichia coli glutaredoxin. Distant homology with thioredoxins in a superfamily of small proteins with a redox-active cystine disulfide/cysteine dithiol." Eur J Biochem 136:223-232. Pubmed: 6352262
  • Hoog, J. O., von Bahr-Lindstrom, H., Jornvall, H., Holmgren, A. (1986). "Cloning and expression of the glutaredoxin (grx) gene of Escherichia coli." Gene 43:13-21. Pubmed: 3530878
  • Kelley, J. J. 3rd, Caputo, T. M., Eaton, S. F., Laue, T. M., Bushweller, J. H. (1997). "Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements." Biochemistry 36:5029-5044. Pubmed: 9125525
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Sodano, P., Chary, K. V., Bjornberg, O., Holmgren, A., Kren, B., Fuchs, J. A., Wuthrich, K. (1991). "Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin. Sequence-specific assignments and secondary structure determination of the oxidized form." Eur J Biochem 200:369-377. Pubmed: 1889405
  • Sodano, P., Xia, T. H., Bushweller, J. H., Bjornberg, O., Holmgren, A., Billeter, M., Wuthrich, K. (1991). "Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin." J Mol Biol 221:1311-1324. Pubmed: 1942053
  • Xia, T. H., Bushweller, J. H., Sodano, P., Billeter, M., Bjornberg, O., Holmgren, A., Wuthrich, K. (1992). "NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins." Protein Sci 1:310-321. Pubmed: 1304339