Glutamine synthetase

Details

Name
Glutamine synthetase
Kind
protein
Synonyms
  • 6.3.1.2
  • Glutamate--ammonia ligase
Gene Name
glnA
UniProtKB Entry
P0A1P6Swiss-Prot
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
NCBI Taxonomy ID
99287
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
Functions
ATP binding / glutamate-ammonia ligase activity
Processes
glutamine biosynthetic process / nitrogen fixation
Components
cytoplasm
General Function
Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
Specific Function
ATP binding
Pfam Domain Function
Signal Regions
Not Available
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
ResourceLink
UniProtKB IDP0A1P6
UniProtKB Entry NameGLNA_SALTY
GenBank Protein ID154090
GenBank Gene IDM14536
PDB ID(s)1F1H, 1F52, 1FPY, 1LGR, 2GLS, 2LGS
KEGG IDstm:STM4007
NCBI Gene ID1255533
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
2-Amino-4-(Hydroxymethyl-Phosphinyl)Butanoic AcidexperimentalunknowntargetDetails