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Escherichia coli K-12 substr. MG1655 Polypeptide: reduced glutaredoxin 1
Inferred from experiment

Gene: grxA Accession Numbers: EG10417 (EcoCyc), b0849, ECK0840

Synonyms: grx, glutaredoxin 1

Regulation Summary Diagram

Regulation summary diagram for grxA

Alternative forms of reduced glutaredoxin 1: oxidized glutaredoxin 1 (extended summary available)

Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH). Glutaredoxins are similar to thioredoxins; both are usually small (9-12 kDa), and both are capable of catalyzing thiol-disulfide exchange reactions. Representatives of at least one of these two protein families have been found in all organisms studied, indicating that proteins of this type are essential for cellular functions.

A main difference between the two is the mechanism for their reduction. Glutaredoxins are reduced by glutathione (GSH), while thioredoxins are reduced by the specific flavoenzyme thioredoxin reductase. An exception is Grx4 which can be reduced by either Grx1 or by thioredoxin reductase [Fernandes05].

Another difference is their role: while thioredoxins are found to be general reductants of protein disulfides, glutaredoxins are better at reducing mixed disulfides between proteins (or low molecular weight thiol-containing compounds) and GSH.

E. coli possesses at least four different glutaredoxins. Grx1, Grx2 and Grx3 all carry the classic dithiol active site CPYC. Grx4 has a monothiol (CGFS) active site [Aslund96, Fernandes05].

Gene Citations: [Tao97]

Locations: cytosol

Map Position: [889,719 <- 889,976] (19.18 centisomes, 69°)
Length: 258 bp / 85 aa

Molecular Weight of Polypeptide: 9.685 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0002893, CGSC:17683, EchoBASE:EB0412, EcoGene:EG10417, EcoliWiki:b0849, ModBase:P68688, OU-Microarray:b0849, PortEco:grxA, Pride:P68688, Protein Model Portal:P68688, RegulonDB:EG10417, SMR:P68688, String:511145.b0849, UniProt:P68688

Relationship Links: InterPro:IN-FAMILY:IPR002109, InterPro:IN-FAMILY:IPR011767, InterPro:IN-FAMILY:IPR011902, InterPro:IN-FAMILY:IPR012336, InterPro:IN-FAMILY:IPR014025, PDB:Structure:1EGO, PDB:Structure:1EGR, PDB:Structure:1GRX, PDB:Structure:1QFN, PDB:Structure:1UPY, PDB:Structure:1UPZ, PDB:Structure:1UQ0, PDB:Structure:1UQ1, PDB:Structure:1UQ2, PDB:Structure:1UQ3, PDB:Structure:1UQ6, PDB:Structure:1UQ7, PDB:Structure:1UQH, PDB:Structure:1UQN, Pfam:IN-FAMILY:PF00462, Prints:IN-FAMILY:PR00160, Prosite:IN-FAMILY:PS00195, Prosite:IN-FAMILY:PS51354

Reactions known to produce the compound:

glutathione-glutaredoxin redox reactions :
2 glutathione + an oxidized glutaredoxin → glutathione disulfide + a reduced glutaredoxin

Reactions known to both consume and produce the compound:

arsenate detoxification II (glutaredoxin) :
arsenate + a reduced glutaredoxin + H+ ↔ arsenite + an oxidized glutaredoxin + H2O

In Reactions of unknown directionality:

Not in pathways:
an oxidized glutaredoxin + 2 e- = a reduced glutaredoxin

Genetic Regulation Schematic

Genetic regulation schematic for grxA

GO Terms:
Biological Process:
Inferred by computational analysisGO:0009263 - deoxyribonucleotide biosynthetic process [UniProtGOA11a]
Inferred by computational analysisGO:0045454 - cell redox homeostasis [GOA01a]
Inferred by computational analysisGO:0055114 - oxidation-reduction process [UniProtGOA11a]
Molecular Function:
Inferred by computational analysisGO:0009055 - electron carrier activity [GOA01a]
Inferred by computational analysisGO:0015035 - protein disulfide oxidoreductase activity [GOA01a]
Cellular Component:
Inferred by computational analysisGO:0005623 - cell [GOA01a]
Inferred by computational analysisGO:0005829 - cytosol [DiazMejia09]

MultiFun Terms: metabolismbiosynthesis of macromolecules (cellular constituents)large molecule carriersthioredoxin, glutaredoxin

Essentiality data for grxA knockouts:

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB LennoxYes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerolYes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucoseYes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]
Yes [Feist07, Comment 3]

Revised 21-Sep-2006 by Caspi R, SRI International

Sequence Features

Protein sequence of reduced glutaredoxin 1 with features indicated

Feature Class Location Citations Comment
Conserved-Region 1 -> 85
Inferred by computational analysis[UniProt15]
UniProt: Glutaredoxin.
Pfam PF00462 4 -> 69
Inferred by computational analysis[Finn14]
Glutaredoxin : Glutaredoxin
Disulfide-Bond-Site 11, 14
Author statement[UniProt15]
UniProt: Redox-active.

Gene Local Context (not to scale -- see Genome Browser for correct scale)

Gene local context diagram

Transcription Units

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b0849 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10417; confirmed by SwissProt match.


Aslund96: Aslund F, Nordstrand K, Berndt KD, 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(12);6736-45. PMID: 8636094

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Fernandes05: Fernandes AP, Fladvad M, Berndt C, Andresen C, Lillig CH, 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(26);24544-52. PMID: 15833738

Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Tao97: Tao K (1997). "oxyR-dependent induction of Escherichia coli grx gene expression by peroxide stress." J Bacteriol 1997;179(18);5967-70. PMID: 9294462

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

Baez13a: Baez A, Shiloach J (2013). "Escherichia coli avoids high dissolved oxygen stress by activation of SoxRS and manganese-superoxide dismutase." Microb Cell Fact 12;23. PMID: 23497217

Zheng01a: Zheng M, Wang X, Templeton LJ, Smulski DR, LaRossa RA, Storz G (2001). "DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide." J Bacteriol 183(15);4562-70. PMID: 11443091

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sat Apr 30, 2016, biocyc11.