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MetaCyc Enzyme: glutamine synthetase adenylyltransferase / glutamine synthetase deadenylase

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

Species: Escherichia coli K-12 substr. MG1655

Summary:
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 [Pahel79a].

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].

Locations: cytosol

Map Position: [3,194,823 <- 3,197,663]

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

Credits:
Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International


Enzymatic reaction of: glutamine synthetase adenylyltransferase

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

EC Number: 2.7.7.42

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.

Credits:
Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

Cofactors or Prosthetic Groups: Mg2+ [Shapiro68]

Activators (Unknown Mechanism): L-glutamine [Kingdon67b]

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

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


Enzymatic reaction of: glutamine synthetase deadenylase

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

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.

Credits:
Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

Cofactors or Prosthetic Groups: Mn2+ [Comment 2]

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

Feature Class Location Citations Comment
Protein-Segment 91 -> 302
[UniProt10a]
UniProt: GlnE 1; Sequence Annotation Type: region of interest;
Sequence-Conflict 524
[vanHeeswijk93, UniProt10]
UniProt: (in Ref. 1; CAA79892);
Protein-Segment 609 -> 830
[UniProt10a]
UniProt: GlnE 2; Sequence Annotation Type: region of interest;
Sequence-Conflict 624 -> 625
[vanHeeswijk93, UniProt10]
UniProt: (in Ref. 1; CAA79892);

History:
10/20/97 Gene b3053 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11602; confirmed by SwissProt match.


References

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

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

Kingdon67b: 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

Pahel79a: 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 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Wed Jul 29, 2015, biocyc12.