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Identification
HMDB Protein ID HMDBP00670
Secondary Accession Numbers
  • 5943
  • HMDBP03880
Name Glutamine synthetase
Synonyms
  1. GS
  2. Glutamate decarboxylase
  3. Glutamate--ammonia ligase
Gene Name GLUL
Protein Type Enzyme
Biological Properties
General Function Involved in glutamate-ammonia ligase activity
Specific Function This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity). Essential for proliferation of fetal skin fibroblasts.
Pathways
  • Alanine, aspartate and glutamate metabolism
  • Ammonia Recycling
  • Arginine and proline metabolism
  • GABAergic synapse
  • Glutamatergic synapse
  • Glyoxylate and dicarboxylate metabolism
Reactions
Adenosine triphosphate + L-Glutamic acid + Ammonia → ADP + Phosphoric acid + L-Glutamine details
L-Glutamic acid → gamma-Aminobutyric acid + CO(2) details
GO Classification
Biological Process
cellular nitrogen compound metabolic process
cell proliferation
neurotransmitter uptake
response to glucose stimulus
glutamine biosynthetic process
glutamate catabolic process
Cellular Component
cytosol
mitochondrion
Function
catalytic activity
ligase activity
acid-ammonia (or amide) ligase activity
ammonia ligase activity
glutamate-ammonia ligase activity
ligase activity, forming carbon-nitrogen bonds
Molecular Function
ATP binding
glutamate-ammonia ligase activity
glutamate decarboxylase activity
Process
metabolic process
nitrogen compound metabolic process
cellular metabolic process
glutamine metabolic process
glutamine family amino acid metabolic process
glutamine biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
Cellular Location
  1. Cytoplasm
  2. Mitochondrion
Gene Properties
Chromosome Location 1
Locus 1q31
SNPs GLUL
Gene Sequence
>1122 bp
ATGACCACCTCAGCAAGTTCCCACTTAAATAAAGGCATCAAGCAGGTGTACATGTCCCTG
CCTCAGGGTGAGAAAGTCCAGGCCATGTATATCTGGATCGATGGTACTGGAGAAGGACTG
CGCTGCAAGACCCGGACCCTGGACAGTGAGCCCAAGTGTGTGGAAGAGTTGCCTGAGTGG
AATTTCGATGGCTCCAGTACTTTACAGTCTGAGGGTTCCAACAGTGACATGTATCTCGTG
CCTGCTGCCATGTTTCGGGACCCCTTCCGTAAGGACCCTAACAAGCTGGTGTTATGTGAA
GTTTTCAAGTACAATCGAAGGCCTGCAGAGACCAATTTGAGGCACACCTGTAAACGGATA
ATGGACATGGTGAGCAACCAGCACCCCTGGTTTGGCATGGAGCAGGAGTATACCCTCATG
GGGACAGATGGGCACCCCTTTGGTTGGCCTTCCAACGGCTTCCCAGGGCCCCAGGGTCCA
TATTACTGTGGTGTGGGAGCAGACAGAGCCTATGGCAGGGACATCGTGGAGGCCCATTAC
CGGGCCTGCTTGTATGCTGGAGTCAAGATTGCGGGGACTAATGCCGAGGTCATGCCTGCC
CAGTGGGAATTTCAGATTGGACCTTGTGAAGGAATCAGCATGGGAGATCATCTCTGGGTG
GCCCGTTTCATCTTGCATCGTGTGTGTGAAGACTTTGGAGTGATAGCAACCTTTGATCCT
AAGCCCATTCCTGGGAACTGGAATGGTGCAGGCTGCCATACCAACTTCAGCACCAAGGCC
ATGCGGGAGGAGAATGGTCTGAAGTACATCGAGGAGGCCATTGAGAAACTAAGCAAGCGG
CACCAGTACCACATCCGTGCCTATGATCCCAAGGGAGGCCTGGACAATGCCCGACGTCTA
ACTGGATTCCATGAAACCTCCAACATCAACGACTTTTCTGGTGGTGTAGCCAATCGTAGC
GCCAGCATACGCATTCCCCGGACTGTTGGCCAGGAGAAGAAGGGTTACTTTGAAGATCGT
CGCCCCTCTGCCAACTGCGACCCCTTTTCGGTGACAGAAGCCCTCATCCGCACGTGTCTT
CTCAATGAAACCGGCGATGAGCCCTTCCAGTACAAAAATTAA
Protein Properties
Number of Residues 373
Molecular Weight 42064.15
Theoretical pI 6.885
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Glutamine synthetase
MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEW
NFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRI
MDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHY
RACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDP
KPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRL
TGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCL
LNETGDEPFQYKN
GenBank ID Protein 31833
UniProtKB/Swiss-Prot ID P15104
UniProtKB/Swiss-Prot Entry Name GLNA_HUMAN
PDB IDs
GenBank Gene ID Y00387
GeneCard ID GLUL
GenAtlas ID GLUL
HGNC ID HGNC:4341
References
General References
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  4. Gibbs CS, Campbell KE, Wilson RH: Sequence of a human glutamine synthetase cDNA. Nucleic Acids Res. 1987 Aug 11;15(15):6293. [PubMed:2888076 ]
  5. Van den Hoff MJ, Geerts WJ, Das AT, Moorman AF, Lamers WH: cDNA sequence of the long mRNA for human glutamine synthase. Biochim Biophys Acta. 1991 Oct 8;1090(2):249-51. [PubMed:1681907 ]
  6. Christa L, Simon MT, Flinois JP, Gebhardt R, Brechot C, Lasserre C: Overexpression of glutamine synthetase in human primary liver cancer. Gastroenterology. 1994 May;106(5):1312-20. [PubMed:7909780 ]
  7. Boksha IS, Schonfeld HJ, Langen H, Muller F, Tereshkina EB, Burbaeva GSh: Glutamine synthetase isolated from human brain: octameric structure and homology of partial primary structure with human liver glutamine synthetase. Biochemistry (Mosc). 2002 Sep;67(9):1012-20. [PubMed:12387715 ]
  8. Vermeulen T, Gorg B, Vogl T, Wolf M, Varga G, Toutain A, Paul R, Schliess F, Haussinger D, Haberle J: Glutamine synthetase is essential for proliferation of fetal skin fibroblasts. Arch Biochem Biophys. 2008 Oct 1;478(1):96-102. doi: 10.1016/j.abb.2008.07.009. Epub 2008 Jul 17. [PubMed:18662667 ]
  9. Olkku A, Mahonen A: Wnt and steroid pathways control glutamate signalling by regulating glutamine synthetase activity in osteoblastic cells. Bone. 2008 Sep;43(3):483-93. doi: 10.1016/j.bone.2008.04.016. Epub 2008 May 7. [PubMed:18555765 ]
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