Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

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Gln-synt_C Glutamine synthetase, catalytic domain

SMART accession number:	SM01230
Description:	-
Interpro abstract (IPR008146):	Glutamine synthetase ( EC 6.3.1.2 ) (GS) [ (PUBMED:2900091) ] plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. There seem to be three different classes of GS [ (PUBMED:8096645) (PUBMED:2575672) (PUBMED:7916055) ]: Class I enzymes (GSI) are specific to prokaryotes, and are oligomers of 12 identical subunits. The activity of GSI-type enzyme is controlled by the adenylation of a tyrosine residue. The adenylated enzyme is inactive (see IPR001637 ). Class II enzymes (GSII) are found in eukaryotes and in bacteria belonging to the Rhizobiaceae, Frankiaceae, and Streptomycetaceae families (these bacteria have also a class-I GS). GSII are octamer of identical subunits. Plants have two or more isozymes of GSII, one of the isozymes is translocated into the chloroplast. Class III enzymes (GSIII) have been found in Bacteroides fragilis. in Butyrivibrio fibrisolvens. It is a hexamer of identical chains and in some protozoa. It is much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. While the three classes of GS's are clearly structurally related, the sequence similarities are not so extensive.
GO process:	nitrogen compound metabolic process (GO:0006807)
GO function:	glutamate-ammonia ligase activity (GO:0004356)
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 49158 Gln-synt_C domains in 49148 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing Gln-synt_C domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Gln-synt_C domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing Gln-synt_C domain in the selected taxonomic class.

• Cellular role (predicted cellular role)

• Cellular role: metabolism
  

• Structure (3D structures containing this domain)

• 3D Structures of Gln-synt_C domains in PDB

  PDB code	Main view	Title
  1f1h		CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM WITH THALLIUM IONS
  1f52		CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM CO-CRYSTALLIZED WITH ADP
  1fpy		CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM WITH INHIBITOR PHOSPHINOTHRICIN
  1hto		CRYSTALLOGRAPHIC STRUCTURE OF A RELAXED GLUTAMINE SYNTHETASE FROM MYCOBACTERIUM TUBERCULOSIS
  1htq		Multicopy crystallographic structure of a relaxed glutamine synthetase from Mycobacterium tuberculosis
  1lgr		INTERACTIONS OF NUCLEOTIDES WITH FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM
  2bvc		Crystal structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition state mimic
  2d3a		Crystal Structure of the Maize Glutamine Synthetase complexed with ADP and Methionine sulfoximine Phosphate
  2d3b		Crystal Structure of the Maize Glutamine Synthetase complexed with AMPPNP and Methionine sulfoximine
  2d3c		Crystal Structure of the Maize Glutamine Synthetase complexed with ADP and Phosphinothricin Phosphate
  2gls		REFINED ATOMIC MODEL OF GLUTAMINE SYNTHETASE AT 3.5 ANGSTROMS RESOLUTION
  2j9i		Lengsin is a survivor of an ancient family of class I glutamine synthetases in eukaryotes that has undergone evolutionary re- engineering for a tissue-specific role in the vertebrate eye lens.
  2lgs		FEEDBACK INHIBITION OF FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM BY GLYCINE, ALANINE, AND SERINE
  2ojw		Crystal structure of human glutamine synthetase in complex with ADP and phosphate
  2qc8		Crystal structure of human glutamine synthetase in complex with ADP and methionine sulfoximine phosphate
  2uu7		Crystal structure of apo glutamine synthetase from dog (Canis familiaris)
  2wgs		Crystal structure of Mycobacterium Tuberculosis Glutamine Synthetase in complex with a purine analogue inhibitor.
  2whi		Crystal structure of Mycobacterium Tuberculosis Glutamine Synthetase in complex with a purine analogue inhibitor and L-methionine-S- sulfoximine phosphate.
  3fky		Crystal structure of the glutamine synthetase Gln1deltaN18 from the yeast Saccharomyces cerevisiae
  3ng0		Crystal Structure of Glutamine Synthetase from Synechocystis sp. PCC 6803
  3o6x		Crystal Structure of the type III Glutamine Synthetase from Bacteroides fragilis
  3zxr		Crystal structure of Mycobacterium Tuberculosis Glutamine Synthetase in complex with tri-substituted imidazole inhibitor (3-(2-tert-butyl- 5-(pyridin-4-yl)-1H-imidazol-4-yl)quinoline) and L-methionine-S- sulfoximine phosphate.
  3zxv		Crystal structure of Mycobacterium Tuberculosis Glutamine Synthetase in complex with tri-substituted imidazole inhibitor (4-(2-tert-butyl- 4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl)pyridin-2-amine) and L- methionine-S-sulfoximine phosphate
  4acf		CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS GLUTAMINE SYNTHETASE IN COMPLEX WITH IMIDAZOPYRIDINE INHIBITOR ((4-(6-BROMO-3-(BUTYLAMINO)IMIDAZO(1,2-A)PYRIDIN-2-YL)PHENOXY) ACETIC ACID) AND L-METHIONINE-S-SULFOXIMINE PHOSPHATE.
  4bax		Crystal structure of glutamine synthetase from Streptomyces coelicolor
  4hpp		Crystal structure of novel glutamine synthase homolog
  4is4		The glutamine synthetase from the dicotyledonous plant M. truncatula is a decamer
  4lnf		B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-Q
  4lni		B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state complex
  4lnk		B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-glutamate-AMPPCP complex
  4lnn		B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of apo form of GS
  4lno		B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: form two of GS-1
  4s0r		4S0R
  4s17		4S17
  4xyc		4XYC
  5dm3		5DM3
  5ldf		5LDF

• Links (links to other resources describing this domain)

• INTERPRO	IPR008146
  PFAM	Gln-synt_C

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