Escherichia coli K-12 substr. MG1655 Enzyme: glutamine synthetase adenylyltransferase / glutamine synthetase deadenylase

Gene: glnE Accession Numbers: EG11602 (EcoCyc), b3053, ECK3043

Regulation Summary Diagram: ?

Regulation summary diagram for glnE

glnE encodes a bifunctional polypeptide having both glutamine synthetase adenylyltransferase (ATase) activity and glutamine synthetase deadenylase activity (ATd). It is believed that there are two separate catalytic sites on the polypeptide [Rhee89].

GlnE catalyzes the ATP-dependent addition of AMP to a subunit of glutamine synthetase, with the release of PPi. In the adenylylation reaction, the AMP moiety of ATP is covalently attached to a unique tyrosyl residue in each of the 12 identical subunits of glutamine synthetase [Garcia83]. Each subunit can be adenylylated so that a molecule of glutamine synthetase can have 12 adenylyl groups covalently attached. Adenylylation of a subunit inactivates that subunit only, unadenylylated subunits remain active. The catalytic activity of glutamine synthetase is regulated by adenylylation; the enzymatic activity of glutamine synthetase is inversely proportional to the number of covalently bound AMP groups [Pahel79].

GlnE catalyzes a phosphorolysis reaction which removes the adenylyl group from the synthetase subunits returning the enzyme to its active state. PII-UMP interacts with ATd as part of a complex regulatory system [Rhee89]

Under anaerobiosis, FNR activates glnE gene expression, but it is not known if this regulation is direct or indirect [Salmon03].

Gene Citations: [vanHeeswijk93]

Locations: cytosol

Map Position: [3,194,823 <- 3,197,663] (68.86 centisomes, 248°)
Length: 2841 bp / 946 aa

Molecular Weight of Polypeptide: 108.42 kD (from nucleotide sequence)

pI: 5.28

Unification Links: ASAP:ABE-0010018 , CGSC:33468 , DIP:DIP-9780N , EchoBASE:EB1559 , EcoGene:EG11602 , EcoliWiki:b3053 , OU-Microarray:b3053 , PortEco:glnE , PR:PRO_000022785 , Pride:P30870 , Protein Model Portal:P30870 , RefSeq:NP_417525 , RegulonDB:EG11602 , SMR:P30870 , String:511145.b3053 , UniProt:P30870

Relationship Links: InterPro:IN-FAMILY:IPR005190 , InterPro:IN-FAMILY:IPR013546 , InterPro:IN-FAMILY:IPR023057 , PDB:Structure:1V4A , PDB:Structure:3K7D , Pfam:IN-FAMILY:PF03710 , Pfam:IN-FAMILY:PF08335

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01, GOA01a]
Molecular Function: GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0000287 - magnesium ion binding Inferred by computational analysis [GOA06]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a]
GO:0008882 - [glutamate-ammonia-ligase] adenylyltransferase activity Inferred by computational analysis [GOA06, GOA01, GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]

MultiFun Terms: information transfer protein related posttranslational modification
metabolism metabolism of other compounds nitrogen metabolism

Essentiality data for glnE 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]

Enzymatic reaction of: glutamine synthetase adenylyltransferase

Synonyms: ATase, glutamate-ammonia-ligase adenylyltransferase, adenylyltransferase, ATP:[L-glutamate:ammonia ligase(ADP-forming)] adenylyltransferase

EC Number:

a [glutamine-synthetase]-L-tyrosine + ATP <=> a [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine + diphosphate

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

The reaction is physiologically favored in the direction shown.

In Pathways: Nitrogen Regulation Two-Component System

Cofactors or Prosthetic Groups: Mg2+ [Shapiro68]

Activators (Unknown Mechanism): L-glutamine [Kingdon67] , PII [Caban76, Comment 4]

Inhibitors (Unknown Mechanism): (S)-malate [Ebner70] , citrate [Ebner70, Comment 5] , oxaloacetate [Ebner70, Comment 5] , coenzyme A [Ebner70, Comment 5] , phosphoenolpyruvate [Ebner70, Comment 5] , 3-phospho-D-glycerate [Ebner70, Comment 5] , fructose 1,6-bisphosphate [Ebner70, Comment 5] , β-D-fructofuranose 6-phosphate [Ebner70, Comment 5] , sulfate [Ebner70a, Helmward89, Comment 5] , diphosphate [Ebner70a, Helmward89, Comment 5] , phosphate [Ebner70a, Helmward89, Comment 5] , 2-oxoglutarate [Ebner70, Ebner70a, Helmward89, Comment 5]

Primary Physiological Regulators of Enzyme Activity: L-glutamine , PII , 2-oxoglutarate

Enzymatic reaction of: glutamine synthetase deadenylase

Synonyms: ATd, adenylyl-[glutamate-ammonia ligase] hydrolase, adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] adenylylhydrolyase

EC Number: 2.7.7.-

a [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine + phosphate <=> a [glutamine-synthetase]-L-tyrosine + ADP

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

The reaction is physiologically favored in the direction shown.

In Pathways: Nitrogen Regulation Two-Component System

Cofactors or Prosthetic Groups: Mn2+ [Comment 6]

Activators (Unknown Mechanism): UTP [Shapiro69] , phosphate [Shapiro69] , arsenate [Shapiro69] , 2-oxoglutarate [Shapiro69, Shapiro68]

Inhibitors (Unknown Mechanism): diphosphate [Shapiro69] , L-glutamine [Shapiro69, Shapiro68]

Primary Physiological Regulators of Enzyme Activity: 2-oxoglutarate , L-glutamine

Sequence Features

Protein sequence of glutamine synthetase adenylyltransferase / glutamine synthetase deadenylase with features indicated

Feature Class Location Citations Comment
Protein-Segment 91 -> 302
UniProt: GlnE 1; Sequence Annotation Type: region of interest;
Sequence-Conflict 524
[vanHeeswijk93, UniProt10a]
UniProt: (in Ref. 1; CAA79892);
Protein-Segment 609 -> 830
UniProt: GlnE 2; Sequence Annotation Type: region of interest;
Sequence-Conflict 624 -> 625
[vanHeeswijk93, UniProt10a]
UniProt: (in Ref. 1; CAA79892);

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b3053 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11602; 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

Caban76: Caban CE, Ginsburg A (1976). "Glutamine synthetase adenylyltransferase from Escherichia coli: purification and physical and chemical properties." Biochemistry 1976;15(7);1569-80. PMID: 4094

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

Ebner70: Ebner E, Wolf D, Gancedo C, Elsasser S, Holzer H (1970). "ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties." Eur J Biochem 1970;14(3);535-44. PMID: 4920894

Ebner70a: Ebner E, Gancedo C, Holzer H "ATP:Glutamine synthetase adenylyltransferase (Escherichia coli B)." Methods in Enzymology 1970; 17A:922-927.

Garcia83: Garcia E, Rhee SG (1983). "Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII uridylyltransferase and uridylyl-removing enzyme." J Biol Chem 1983;258(4);2246-53. PMID: 6130097

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

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

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

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Helmward89: Helmward Z "Handbook of Enzyme Inhibitors. 2nd, revised and enlarged edition." Weinheim, Federal Republic of Germany ; New York, NY, USA , 1989.

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

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

Kingdon67: Kingdon HS, Shapiro BM, Stadtman ER (1967). "Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase." Proc Natl Acad Sci U S A 1967;58(4);1703-10. PMID: 4867671

Pahel79: Pahel G, Tyler B (1979). "A new glnA-linked regulatory gene for glutamine synthetase in Escherichia coli." Proc Natl Acad Sci U S A 1979;76(9);4544-8. PMID: 41243

Rhee89: Rhee SG, Chock PB, Stadtman ER (1989). "Regulation of Escherichia coli glutamine synthetase." Adv Enzymol Relat Areas Mol Biol 1989;62;37-92. PMID: 2567108

Salmon03: Salmon K, Hung SP, Mekjian K, Baldi P, Hatfield GW, Gunsalus RP (2003). "Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR." J Biol Chem 278(32);29837-55. PMID: 12754220

Shapiro68: Shapiro BM, Stadtman ER (1968). "Glutamine synthetase deadenylylating enzyme." Biochem Biophys Res Commun 1968;30(1);32-7. PMID: 4866293

Shapiro69: Shapiro BM (1969). "The glutamine synthetase deadenylylating enzyme system from Escherichia coli. Resolution into two components, specific nucleotide stimulation, and cofactor requirements." Biochemistry 8(2);659-70. PMID: 4893578

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

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

vanHeeswijk93: van Heeswijk WC, Rabenberg M, Westerhoff HV, Kahn D (1993). "The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli." Mol Microbiol 9(3);443-57. PMID: 8412694

Other References Related to Gene Regulation

Kumar11: Kumar R, Shimizu K (2011). "Transcriptional regulation of main metabolic pathways of cyoA, cydB, fnr, and fur gene knockout Escherichia coli in C-limited and N-limited aerobic continuous cultures." Microb Cell Fact 10;3. PMID: 21272324

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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