Identification
Name:Glutaredoxin-2
Synonyms:
  • Grx2
Gene Name:grxB
Enzyme Class:Not Available
Biological Properties
General Function:Involved in protein binding
Specific Function:Involved in reducing some disulfides in a coupled system with glutathione reductase. Does not act as hydrogen donor for ribonucleotide reductase
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Complex Reactions:
glutaredoxin+ThumbThumb+glutaredoxin+Thumb
glutaredoxin + Uridine 5'-diphosphatedUDP + glutaredoxin + Water
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Thumb+glutaredoxinThumb+glutaredoxin+Thumb
Guanosine diphosphate + glutaredoxin → dGDP + glutaredoxin + Water
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Thumb+glutaredoxinThumb+glutaredoxin+Thumb
CDP + glutaredoxin → dCDP + glutaredoxin + Water
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Thumb+glutaredoxinThumb+glutaredoxin+Thumb
ADP + glutaredoxin → dADP + glutaredoxin + Water
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glutaredoxin+Thumbglutaredoxin+2 Thumb+Thumb+Thumb
glutaredoxin+2 Thumbglutaredoxin+Thumb
glutaredoxin + 2 Glutathione → glutaredoxin + Glutathione disulfide
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Thumb+2 ThumbThumb+Thumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB00061Adenosine 3',5'-diphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21394ArsenateMetaboCard
ECMDB21309ArseniteMetaboCard
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:b1064
Gene OrientationCounterclockwise
Centisome Percentage:24.20
Left Sequence End1122630
Right Sequence End1123277
Gene Sequence:
>648 bp
ATGGCACGAAAAACCAAACAAGAAGCGCAAGAAACGCGCCAACACATCCTCGATGTGGCT
CTACGTCTTTTCTCACAGCAGGGGGTATCATCCACCTCGCTGGGCGAGATTGCAAAAGCA
GCTGGCGTTACGCGCGGTGCAATCTACTGGCATTTTAAAGACAAGTCGGATTTGTTCAGT
GAGATCTGGGAACTGTCAGAATCCAATATTGGTGAACTAGAGCTTGAGTATCAGGCAAAA
TTCCCTGGCGATCCACTCTCAGTATTAAGAGAGATATTAATTCATGTTCTTGAATCCACG
GTGACAGAAGAACGGCGTCGATTATTGATGGAGATTATATTCCACAAATGCGAATTTGTC
GGAGAAATGGCTGTTGTGCAACAGGCACAACGTAATCTCTGTCTGGAAAGTTATGACCGT
ATAGAACAAACGTTAAAACATTGTATTGAAGCGAAAATGTTGCCTGCGGATTTAATGACG
CGTCGCGCAGCAATTATTATGCGCGGCTATATTTCCGGCCTGATGGAAAACTGGCTCTTT
GCCCCGCAATCTTTTGATCTTAAAAAAGAAGCCCGCGATTACGTTGCCATCTTACTGGAG
ATGTATCTCCTGTGCCCCACGCTTCGTAATCCTGCCACTAACGAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:215
Protein Molecular Weight:24350
Protein Theoretical pI:8
PDB File:1G7O
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glutaredoxin-2
MKLYIYDHCPYCLKARMIFGLKNIPVELHVLLNDDAETPTRMVGQKQVPILQKDDSRYMP
ESMDIVHYVDKLDGKPLLTGKRSPAIEEWLRKVNGYANKLLLPRFAKSAFDEFSTPAARK
YFVDKKEASAGNFADLLAHSDGLIKNISDDLRALDKLIVKPNAVNGELSEDDIQLFPLLR
NLTLVAGINWPSRVADYRDNMAKQTQINLLSSMAI
References
External Links:
ResourceLink
Uniprot ID:P0AC59
Uniprot Name:GLRX2_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674603
PDB ID:1G7O
Ecogene ID:EG12688
Ecocyc:EG12688
ColiBase:b1064
Kegg Gene:b1064
EchoBASE ID:EB2551
CCDB:GLRX2_ECOLI
BacMap:16129027
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
  • 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
  • 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
  • Vlamis-Gardikas, A., Aslund, F., Spyrou, G., Bergman, T., Holmgren, A. (1997). "Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli." J Biol Chem 272:11236-11243. Pubmed: 9111025