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Escherichia coli K-12 substr. MG1655 Enzyme: arsenate reductase



Gene: arsC Accession Numbers: EG12237 (EcoCyc), b3503, ECK3488

Synonyms: arsG

Regulation Summary Diagram: ?

Summary:
Based on sequence similarity with the R773-plasmid encoded arsenite resistance operon, ArsB is a transporter and ArsC is an arsenate reductase [Carlin95]. The chromosomally encoded operon, however, is lacking arsA, which encodes a putative ATP-binding protein. Deletion mutants of the chromosomal arsRBC operon exhibit 10-20 times more sensitivity to arsenite and 5-10 times more selectivity to antimonite and arsenate than the parent strain. Expression of the cloned arsRBC conferred increased arsenite resistance compared with wild-type [Carlin95].

Arsenate reductase catalyzes the reduction of arsenate to arsenite using glutathione with glutaredoxin as electron donors. The resulting arsenite is then quickly removed from the cell via the ArsB transport protein.

The reaction takes place in several steps. Arsenate binds to the enzyme and is reduced by electrons donated from both the enzyme and glutathione. Glutaredoxin then reduces the enzyme-glutathione disulfide and is in turn regenerated by glutathione. The oxidized glutathione is finally reduced by glutathione reductase. All three glutaredoxins in E. coli can participate in the arsenate reductase reaction, but glutaredoxin 2 appears the most effective. [Shi99b, Liu97b, Cai96, Diorio95]

Locations: cytosol

Map Position: [3,648,260 -> 3,648,685] (78.63 centisomes)
Length: 426 bp / 141 aa

Molecular Weight of Polypeptide: 15.853 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0011439 , CGSC:35999 , EchoBASE:EB2149 , EcoGene:EG12237 , EcoliWiki:b3503 , ModBase:P0AB96 , OU-Microarray:b3503 , PortEco:arsC , PR:PRO_000022155 , Pride:P0AB96 , Protein Model Portal:P0AB96 , RefSeq:NP_417960 , RegulonDB:EG12237 , SMR:P0AB96 , String:511145.b3503 , Swiss-Model:P0AB96 , UniProt:P0AB96

Relationship Links: InterPro:IN-FAMILY:IPR006659 , InterPro:IN-FAMILY:IPR006660 , InterPro:IN-FAMILY:IPR012336 , PDB:Structure:1I9D , Pfam:IN-FAMILY:PF03960 , Prosite:IN-FAMILY:PS51353

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0046685 - response to arsenic-containing substance Inferred by computational analysis [UniProtGOA11]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0008794 - arsenate reductase (glutaredoxin) activity Inferred by computational analysis [GOA01a, GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: cell processes protection drug resistance/sensitivity

Essentiality data for arsC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Enzymatic reaction of: arsenate reductase

Synonyms: arsenical pump modifier

EC Number: 1.20.4.1

arsenate + a reduced glutaredoxin + H+ <=> arsenite + an oxidized glutaredoxin + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

In Pathways: arsenate detoxification II (glutaredoxin)

Summary:
Arsenate reductase catalyzes the reduction of arsenate to arsenite using glutathione with glutaredoxin as electron donors. The resulting arsenite is then quickly removed from the cell via the ArsB transport protein.

The reaction takes place in several steps. Arsenate binds to the enzyme and is reduced by electrons donated from both the enzyme and glutathione. Glutaredoxin then reduces the enzyme-glutathione disulfide and is in turn regenerated by glutathione. The oxidized glutathione is finally reduced by glutathione reductase.

All three glutaredoxins in E. coli can participate in the arsenate reductase reaction, but glutaredoxin 2 appears the most effective. [Shi99b, Liu97b, Cai96, Diorio95]

Kinetic Parameters:

Substrate
Km (μM)
Citations
arsenate
8000.0
[Gladysheva94, BRENDA14]

pH(opt): 6.3 [BRENDA14, Gladysheva94]


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b3503 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12237; confirmed by SwissProt match.


References

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

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Cai96: Cai J, DuBow MS (1996). "Expression of the Escherichia coli chromosomal ars operon." Can J Microbiol 1996;42(7);662-71. PMID: 8764681

Carlin95: Carlin A, Shi W, Dey S, Rosen BP (1995). "The ars operon of Escherichia coli confers arsenical and antimonial resistance." J Bacteriol 1995;177(4);981-6. PMID: 7860609

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

Diorio95: Diorio C, Cai J, Marmor J, Shinder R, DuBow MS (1995). "An Escherichia coli chromosomal ars operon homolog is functional in arsenic detoxification and is conserved in gram-negative bacteria." J Bacteriol 1995;177(8);2050-6. PMID: 7721697

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

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Gladysheva94: Gladysheva TB, Oden KL, Rosen BP (1994). "Properties of the arsenate reductase of plasmid R773." Biochemistry 33(23);7288-93. PMID: 8003492

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

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

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Liu97b: Liu J, Rosen BP (1997). "Ligand interactions of the ArsC arsenate reductase." J Biol Chem 1997;272(34);21084-9. PMID: 9261111

Shi99b: Shi J, Vlamis-Gardikas A, Aslund F, Holmgren A, Rosen BP (1999). "Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction." J Biol Chem 1999;274(51);36039-42. PMID: 10593884

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

Busenlehner03: Busenlehner LS, Pennella MA, Giedroc DP (2003). "The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance." FEMS Microbiol Rev 27(2-3);131-43. PMID: 12829264

Xu96d: Xu C, Shi W, Rosen BP (1996). "The chromosomal arsR gene of Escherichia coli encodes a trans-acting metalloregulatory protein." J Biol Chem 1996;271(5);2427-32. PMID: 8576202


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 SRI International Pathway Tools version 18.5 on Fri Nov 28, 2014, biocyc14.