|Gene:||arsC||Accession Numbers: EG12237 (EcoCyc), b3503, ECK3488|
Based on sequence similarity with the R773-encoded enzyme, ArsC is thought to catalyze the reduction of arsenate to arsenite using glutathione with glutaredoxin as electron donors. The resulting arsenite is then removed from the cell via the ArsB transport protein.
Unlike the chromosomally-encoded ArsC described here, the R773 plasmid-encoded enzyme has been studied experimentally. The arsenate reductase reaction involves sequential action of three different thiolate nucleophiles that function as a redox cascade [Messens06]. All three glutaredoxins in E. coli can participate in the arsenate reductase reaction, but glutaredoxin 2 appears the most effective [Shi99]. Crystal structures of ArsC have been solved [Martin01, DeMel04], and residues involved in arsenate binding and transition-state stabilization were identified [Shi03, DeMel04].
Based on sequence similarity with the R773-plasmid encoded arsenite resistance operon, ArsB is a transporter and ArsC is an arsenate reductase [Diorio95, Carlin95]. The chromosomally encoded operon, however, is lacking arsA, which encodes a putative ATP-binding protein.
Expression of arsRBC is induced by exposure to arsenite [Diorio95, Carlin95]; transcription is negatively regulated by ArsR [Cai96]. arsRBC mutants are more sensitive to sodium arsenate and arsenite than wild type, while overexpression of arsRBC from a plasmid leads to increased arsenate, arsenite and antimonite resistance [Diorio95, Carlin95]. ΔarsRBC mutant accumulates significantly more intracellular arsenite than wild type [Carlin95].
|Map Position: [3,648,260 -> 3,648,685] (78.63 centisomes, 283°)||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
|Biological Process:||GO:0006974 - cellular response to DNA damage stimulus
GO:0046685 - response to arsenic-containing substance [UniProtGOA11, Carlin95, Diorio95]
GO:0055114 - oxidation-reduction process [UniProtGOA11, GOA01]
|Molecular Function:||GO:0008794 - arsenate reductase (glutaredoxin) activity
[GOA01a, GOA01, Carlin95]
GO:0016491 - oxidoreductase activity [UniProtGOA11]
|Cellular Component:||GO:0005829 - cytosol [DiazMejia09]|
|MultiFun Terms:||cell processes → protection → detoxification|
|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: 18.104.22.168
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)
10/20/97 Gene b3503 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12237; confirmed by SwissProt match.
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
Chaturvedi14: Chaturvedi N, Pandey PN (2014). "Phylogenetic analysis of gammaproteobacterial arsenate reductase proteins specific to Enterobacteriaceae family, signifying arsenic toxicity." Interdiscip Sci 6(1);57-62. PMID: 24464705
DeMel04: DeMel S, Shi J, Martin P, Rosen BP, Edwards BF (2004). "Arginine 60 in the ArsC arsenate reductase of E. coli plasmid R773 determines the chemical nature of the bound As(III) product." Protein Sci 13(9);2330-40. PMID: 15295115
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
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
Martin01: Martin P, DeMel S, Shi J, Gladysheva T, Gatti DL, Rosen BP, Edwards BF (2001). "Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme." Structure 9(11);1071-81. PMID: 11709171
Rosen02: Rosen BP (2002). "Transport and detoxification systems for transition metals, heavy metals and metalloids in eukaryotic and prokaryotic microbes." Comp Biochem Physiol A Mol Integr Physiol 133(3);689-93. PMID: 12443926
Shi03: Shi J, Mukhopadhyay R, Rosen BP (2003). "Identification of a triad of arginine residues in the active site of the ArsC arsenate reductase of plasmid R773." FEMS Microbiol Lett 227(2);295-301. PMID: 14592722
Shi99: 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
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
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