Glutaredoxin-4 (P0AC69)

Identification
Name:Glutaredoxin-4
Synonyms:
  • Grx4
  • Monothiol glutaredoxin
Gene Name:grxD
Enzyme Class:Not Available
Biological Properties
General Function:Involved in electron carrier activity
Specific Function:Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (Probable)
Cellular Location:Cytoplasm
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:b1654
Gene OrientationCounterclockwise
Centisome Percentage:37.33
Left Sequence End1731778
Right Sequence End1732125
Gene Sequence:
>348 bp
ATGGCTATCATCCCAAAAAACTATGCGCGGTTAGAAAGCGGCTATCGCGAAAAAGCATTA
AAAATCTATCCGTGGGTCTGCGGTCGCTGTTCCCGCGAGTTTGTTTATTCCAACCTGCGT
GAACTTACCGTTCACCACATTGATCACGACCATACCAATAACCCGGAAGATGGCAGTAAC
TGGGAATTGTTGTGTCTCTATTGCCACGATCATGAGCATTCGAAATATACCGAAGCGGAT
CAGTATGGTACGACCGTTATCGCAGGGGAAGATGCGCAGAAAGATGTCGGTGAAGCGAAG
TACAACCCATTCGCTGACCTGAAAGCGATGATGAACAAGAAGAAGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:115
Protein Molecular Weight:12879
Protein Theoretical pI:4
PDB File:1YKA
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glutaredoxin-4
MSTTIEKIQRQIAENPILLYMKGSPKLPSCGFSAQAVQALAACGERFAYVDILQNPDIRA
ELPKYANWPTFPQLWVDGELVGGCDIVIEMYQRGELQQLIKETAAKYKSEEPDAE
References
External Links:
ResourceLink
Uniprot ID:P0AC69
Uniprot Name:GLRX4_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674550
PDB ID:1YKA
Ecogene ID:EG12181
Ecocyc:EG12181
ColiBase:b1654
Kegg Gene:b1654
EchoBASE ID:EB2098
CCDB:GLRX4_ECOLI
BacMap:16129612
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • Fernandes, A. P., Fladvad, M., Berndt, C., Andresen, C., Lillig, C. H., Neubauer, P., Sunnerhagen, M., Holmgren, A., Vlamis-Gardikas, A. (2005). "A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase." J Biol Chem 280:24544-24552. Pubmed: 15833738
  • Fladvad, M., Bellanda, M., Fernandes, A. P., Mammi, S., Vlamis-Gardikas, A., Holmgren, A., Sunnerhagen, M. (2005). "Molecular mapping of functionalities in the solution structure of reduced Grx4, a monothiol glutaredoxin from Escherichia coli." J Biol Chem 280:24553-24561. Pubmed: 15840565
  • 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
  • Iwema, T., Picciocchi, A., Traore, D. A., Ferrer, J. L., Chauvat, F., Jacquamet, L. (2009). "Structural basis for delivery of the intact [Fe2S2] cluster by monothiol glutaredoxin." Biochemistry 48:6041-6043. Pubmed: 19505088
  • Reuven, N. B., Koonin, E. V., Rudd, K. E., Deutscher, M. P. (1995). "The gene for the longest known Escherichia coli protein is a member of helicase superfamily II." J Bacteriol 177:5393-5400. Pubmed: 7559321