ECMDB: 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

1.0

→

1.0

1.0glutaredoxin

1.0

1.0glutaredoxin + 1.0Uridine 5'-diphosphate → 1.0dUDP + 1.0glutaredoxin + 1.0Water
ReactionCard

1.0

1.0glutaredoxin

→

1.0

1.0glutaredoxin

1.0

1.0Guanosine diphosphate + 1.0glutaredoxin → 1.0dGDP + 1.0glutaredoxin + 1.0Water
ReactionCard

1.0

1.0glutaredoxin

→

1.0

1.0glutaredoxin

1.0

1.0CDP + 1.0glutaredoxin → 1.0dCDP + 1.0glutaredoxin + 1.0Water
ReactionCard

1.0

1.0glutaredoxin

→

1.0

1.0glutaredoxin

1.0

1.0ADP + 1.0glutaredoxin → 1.0dADP + 1.0glutaredoxin + 1.0Water
ReactionCard

1.0glutaredoxin

1.0

→

1.0glutaredoxin

2.0

1.0

1.0glutaredoxin + 1.0Phosphoadenosine phosphosulfate → 1.0glutaredoxin + 2.0Hydrogen ion + 1.0Adenosine 3',5'-diphosphate + 1.0Sulfite
ReactionCard

1.0glutaredoxin

2.0

→

1.0glutaredoxin

1.0

1.0glutaredoxin + 2.0Glutathione → 1.0glutaredoxin + 1.0Glutathione disulfide
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB00061	Adenosine 3',5'-diphosphate	MetaboCard
ECMDB01341	ADP	MetaboCard
ECMDB01546	CDP	MetaboCard
ECMDB21326	dADP	MetaboCard
ECMDB01245	dCDP	MetaboCard
ECMDB00960	dGDP	MetaboCard
ECMDB01000	dUDP	MetaboCard
ECMDB00125	Glutathione	MetaboCard
ECMDB21221	Glutathione disulfide	MetaboCard
ECMDB01201	Guanosine diphosphate	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB01134	Phosphoadenosine phosphosulfate	MetaboCard
ECMDB00240	Sulfite	MetaboCard
ECMDB00295	Uridine 5'-diphosphate	MetaboCard
ECMDB00494	Water	MetaboCard

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 Orientation

Counterclockwise

Centisome Percentage:

81.52

Left Sequence End

3782214

Right Sequence End

3782465

Gene Sequence:

>252 bp
ATGGCCAATGTTGAAATCTATACCAAAGAAACCTGCCCGTATTGCCATCGTGCAAAAGCA
CTGCTGAGCAGCAAGGGCGTGAGTTTCCAGGAGCTGCCGATCGATGGCAACGCCGCCAAG
CGTGAAGAGATGATCAAACGCAGCGGTCGCACCACGGTTCCCCAGATTTTTATTGACGCA
CAGCACATTGGCGGCTGTGATGACTTGTATGCATTGGATGCACGTGGTGGACTGGATCCC
CTGCTGAAATAA

Protein Properties

Pfam Domain Function:

Glutaredoxin (PF00462 )

Protein Residues:

Protein Molecular Weight:

9137

Protein Theoretical pI:

PDB File:

1FOV

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Glutaredoxin-3
MANVEIYTKETCPYCHRAKALLSSKGVSFQELPIDGNAAKREEMIKRSGRTTVPQIFIDA
QHIGGCDDLYALDARGGLDPLLK

References

External Links:

Resource	Link
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