Glutamine synthetase
Details
- Name
- Glutamine synthetase
- Synonyms
- 6.3.1.2
- Glutamate--ammonia ligase
- Gene Name
- glnA
- Organism
- Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
- Amino acid sequence
>lcl|BSEQ0016600|Glutamine synthetase MSAEHVLTMLNEHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFDGSSIGGWKG INESDMVLMPDASTAVIDPFFADSTLIIRCDILEPGTLQGYDRDPRSIAKRAEDYLRATG IADTVLFGPEPEFFLFDDIRFGASISGSHVAIDDIEGAWNSSTKYEGGNKGHRPGVKGGY FPVPPVDSAQDIRSEMCLVMEQMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYK YVVHNVAHRFGKTATFMPKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALYYIG GVIKHAKAINALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRIPVVASPKARRIEVR FPDPAANPYLCFAALLMAGLDGIKNKIHPGEAMDKNLYDLPPEEAKEIPQVAGSLEEALN ALDLDREFLKAGGVFTDEAIDAYIALRREEDDRVRMTPHPVEFELYYSV
- Number of residues
- 469
- Molecular Weight
- 51785.27
- Theoretical pI
- 5.34
- GO Classification
- FunctionsATP binding / glutamate-ammonia ligase activityProcessesglutamine biosynthetic process / nitrogen fixationComponentscytoplasm
- General Function
- Glutamate-ammonia ligase activity
- Specific Function
- Not Available
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0016601|Glutamine synthetase (glnA) ATGTCCGCTGAACACGTTTTGACGATGCTGAACGAGCACGAAGTGAAGTTTGTCGATCTG CGCTTCACCGATACCAAAGGCAAAGAACAGCACGTCACGATTCCTGCTCATCAGGTAAAT GCCGAATTCTTTGAAGAAGGCAAAATGTTTGACGGCTCCTCTATCGGCGGCTGGAAAGGC ATTAACGAATCCGACATGGTGCTGATGCCCGATGCGTCCACTGCGGTTATCGACCCGTTC TTCGCGGACTCCACCCTGATTATCCGTTGTGACATCCTGGAGCCTGGCACTCTGCAAGGT TATGACCGTGACCCACGTTCCATCGCAAAACGTGCGGAAGACTACCTGCGCGCGACCGGT ATCGCCGATACCGTCCTGTTTGGGCCGGAACCTGAATTCTTCCTGTTCGACGACATCCGC TTCGGCGCATCTATCTCCGGCTCACATGTGGCGATTGACGATATTGAAGGCGCCTGGAAC TCCTCTACCAAGTACGAAGGCGGCAACAAAGGCCATCGTCCGGGCGTGAAAGGCGGTTAT TTCCCGGTTCCGCCAGTTGACTCCGCGCAGGATATCCGTTCTGAAATGTGTCTGGTCATG GAGCAGATGGGCCTGGTCGTTGAAGCGCACCACCACGAAGTAGCGACCGCAGGTCAGAAC GAAGTGGCGACCCGCTTTAACACCATGACCAAAAAAGCCGACGAAATTCAGATTTACAAA TATGTCGTGCATAACGTGGCTCACCGCTTCGGTAAGACCGCGACCTTTATGCCAAAACCG ATGTTCGGCGATAACGGTTCCGGTATGCACTGCCACATGTCTCTGGCGAAGAACGGCACC AACCTGTTCTCTGGCGACAAATATGCCGGCCTGTCTGAACAAGCGCTGTACTACATCGGC GGCGTCATCAAACACGCCAAAGCCATCAACGCCCTGGCGAACCCGACCACCAACTCCTAC AAGCGTCTGGTCCCGGGTTACGAAGCGCCGGTGATGCTGGCCTACTCCGCCCGTAACCGT TCCGCCTCCATCCGTATTCCGGTGGTGGCGTCTCCGAAAGCGCGCCGTATCGAAGTTCGC TTCCCGGACCCGGCGGCTAACCCGTATCTGTGCTTTGCCGCCCTGCTGATGGCCGGTCTG GACGGGATTAAGAATAAGATTCACCCGGGCGAAGCCATGGACAAAAACCTGTATGACCTG CCGCCGGAAGAAGCGAAAGAGATCCCACAGGTAGCGGGTTCTCTGGAAGAAGCGCTGAAC GCGCTGGACCTGGACCGCGAGTTCCTGAAAGCAGGCGGCGTGTTCACTGATGAAGCGATC GATGCGTATATTGCGCTGCGTCGCGAAGAAGATGACCGCGTGCGTATGACCCCGCACCCG GTAGAGTTTGAGCTGTACTACAGCGTTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A1P6 UniProtKB Entry Name GLNA_SALTY GenBank Protein ID 154090 GenBank Gene ID M14536 - General References
- Janson CA, Kayne PS, Almassy RJ, Grunstein M, Eisenberg D: Sequence of glutamine synthetase from Salmonella typhimurium and implications for the protein structure. Gene. 1986;46(2-3):297-300. [Article]
- McClelland M, Sanderson KE, Spieth J, Clifton SW, Latreille P, Courtney L, Porwollik S, Ali J, Dante M, Du F, Hou S, Layman D, Leonard S, Nguyen C, Scott K, Holmes A, Grewal N, Mulvaney E, Ryan E, Sun H, Florea L, Miller W, Stoneking T, Nhan M, Waterston R, Wilson RK: Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature. 2001 Oct 25;413(6858):852-6. [Article]
- Yamashita MM, Almassy RJ, Janson CA, Cascio D, Eisenberg D: Refined atomic model of glutamine synthetase at 3.5 A resolution. J Biol Chem. 1989 Oct 25;264(30):17681-90. [Article]
- Gill HS, Eisenberg D: The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition. Biochemistry. 2001 Feb 20;40(7):1903-12. [Article]