Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

MetaCyc Enzyme: glutamine synthetase adenylyltransferase / glutamine synthetase deadenylase

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

Species: Escherichia coli K-12 substr. MG1655

Summary:
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: ?

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: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 16-Sep-2014 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 synthase] + ATP <=> adenylyl-[glutamine synthase] + 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 16-Sep-2014 by Paley S , SRI International

Summary:
Adenylyltransferase (ATase) 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 thus regulated by this adenylylation. The enzymatic activity of glutamine synthetase is inversely proportional to the number of covalently bound AMP groups [Pahel79]. The glnE gene codes for a bifunctional polypeptide having both the ATase activity and the deadenylylation activity (ATd). It is believed that there are two separate catalytic sites on the polypeptide. [Rhee89]

Cofactors or Prosthetic Groups: Mg2+ [Shapiro68a]

Activators (Unknown Mechanism): L-glutamine [Kingdon67b] , PII [Caban76, Comment 1]

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

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

adenylyl-[glutamine synthase] + phosphate <=> [a glutamine synthase] + 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 16-Sep-2014 by Paley S , SRI International

Summary:
Glutamine synthetase deadenylylating enzyme (ATd) 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. The glnE gene codes for a bifunctional polypeptide having both the deadenylylation activity (ATd) and the adenylylating activity (ATase). It is believed that there are two separate catalytic sites on the polypeptide. [Rhee89]

Cofactors or Prosthetic Groups: Mn2+ [Comment 3]

Activators (Unknown Mechanism): UTP [Shapiro69] , phosphate [Shapiro69] , arsenate [Shapiro69] , 2-oxoglutarate [Shapiro69, Shapiro68a]

Inhibitors (Unknown Mechanism): diphosphate [Shapiro69] , L-glutamine [Shapiro69, Shapiro68a]

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


Sequence Features

Feature Class Location Citations Comment
Protein-Segment 91 -> 302
[UniProt, 2010]
UniProt: GlnE 1; Sequence Annotation Type: region of interest;
Sequence-Conflict 524
[vanHeeswijk93, UniProt10]
Alternate sequence: missing; UniProt: (in Ref. 1; CAA79892);
Protein-Segment 609 -> 830
[UniProt, 2010]
UniProt: GlnE 2; Sequence Annotation Type: region of interest;
Sequence-Conflict 624 -> 625
[vanHeeswijk93, UniProt10]
Alternate sequence: PV; 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

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

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

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

Shapiro68a: 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

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

UniProt10: 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


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 18.5 on Tue Nov 25, 2014, BIOCYC14B.