Canmetcon
Identification
Name:Aspartate--ammonia ligase
Synonyms:
  • Asparagine synthetase A
Gene Name:asnA
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:ATP + L-aspartate + NH(3) = AMP + diphosphate + L-asparagine
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb+Thumb
SMPDB Reactions:
Thumb+L-Aspartic acid+Thumb+ThumbThumb+L-Asparagine+Pyrophosphate+Thumb
Adenosine triphosphate + L-Aspartic acid + Ammonia + L-Aspartic acidAdenosine monophosphate + L-Asparagine + Pyrophosphate + L-Asparagine
ReactionCard
L-Aspartic acid+Thumb+Thumb+ThumbL-Asparagine+Thumb+Pyrophosphate+Thumb+Thumb
EcoCyc Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Complex Reactions:
Thumb+Thumb+ThumbThumb+Thumb+Thumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00168L-AsparagineMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
acid-ammonia (or amide) ligase activity
adenyl nucleotide binding
adenyl ribonucleotide binding
aminoacyl-tRNA ligase activity
ammonia ligase activity
aspartate-ammonia ligase activity
ATP binding
binding
catalytic activity
ligase activity
ligase activity, forming aminoacyl-tRNA and related compounds
ligase activity, forming carbon-nitrogen bonds
ligase activity, forming carbon-oxygen bonds
nucleoside binding
nucleotide binding
purine nucleoside binding
Process
asparagine biosynthetic process
asparagine metabolic process
aspartate family amino acid metabolic process
biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular macromolecule biosynthetic process
cellular macromolecule metabolic process
cellular metabolic process
macromolecule biosynthetic process
macromolecule metabolic process
metabolic process
ncRNA metabolic process
RNA metabolic process
translation
tRNA aminoacylation
tRNA aminoacylation for protein translation
tRNA metabolic process
Gene Properties
Blattner:b3744
Gene OrientationClockwise
Centisome Percentage:84.60
Left Sequence End3925178
Right Sequence End3926170
Gene Sequence:
>993 bp
ATGCAGAGCGATAAAGTGCTCAATTTGCCGGCAGGCTACTTTGGTATTGTGTTGGGGACG
ATAGGGATGGGATTTGCCTGGCGCTATGCCAGCCAGGTTTGGCAGGTCAGCCACTGGTTA
GGGGATGGGCTGGTGATTCTGGCGATGATCATCTGGGGATTATTGACTAGCGCATTTATT
GCCCGACTCATACGCTTTCCGCATAGCGTGCTGGCGGAAGTTCGCCATCCAGTGCTGAGC
AGTTTTGTGAGTTTGTTTCCGGCAACGACGATGCTGGTGGCGATTGGTTTTGTTCCGTGG
TTTCGCCCACTGGCGGTGTGCCTGTTCAGTTTTGGTGTCGTGGTTCAGTTGGCTTATGCC
GCCTGGCAAACTGCGGGATTATGGCGCGGATCTCACCCTGAAGAAGCTACCACGCCTGGA
CTGTATCTGCCGACAGTTGCCAACAACTTTATCAGCGCAATGGCCTGTGGTGCGTTGGGC
TACACCGACGCCGGTCTGGTGTTTTTAGGCGCAGGCGTTTTCTCATGGCTAAGCCTTGAA
CCGGTGATCTTGCAGCGTCTGCGCAGTTCGGGAGAATTACCCACGGCACTGCGGACATCA
CTCGGCATTCAGCTCGCTCCTGCGCTGGTGGCTTGTAGTGCCTGGCTGAGCGTCAACGGC
GGCGAGGGTGACACGCTGGCGAAAATGCTTTTCGGTTATGGACTGCTGCAACTGCTGTTT
ATGCTACGTCTGATGCCATGGTATCTCTCCCAGCCATTTAATGCTTCATTCTGGAGTTTC
TCGTTCGGCGTATCTGCACTGGCAACCACCGGTTTGCATCTGGGGAGTGGCAGCGATAAT
GGATTTTTCCATACGCTGGCGGTGCCGCTGTTTATCTTTACCAATTTTATTATTGCAATA
CTGCTCATCCGTACTTTTGCGCTTCTGATGCAGGGAAAATTGTTAGTCAGAACCGAGCGC
GCCGTTTTAATGAAAGCAGAGGACAAAGAATGA
Protein Properties
Pfam Domain Function:
Protein Residues:330
Protein Molecular Weight:36650
Protein Theoretical pI:6
PDB File:12AS
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Aspartate--ammonia ligase
MKTAYIAKQRQISFVKSHFSRQLEERLGLIEVQAPILSRVGDGTQDNLSGCEKAVQVKVK
ALPDAQFEVVHSLAKWKRQTLGQHDFSAGEGLYTHMKALRPDEDRLSPLHSVYVDQWDWE
RVMGDGERQFSTLKSTVEAIWAGIKATEAAVSEEFGLAPFLPDQIHFVHSQELLSRYPDL
DAKGRERAIAKDLGAVFLVGIGGKLSDGHRHDVRAPDYDDWSTPSELGHAGLNGDILVWN
PVLEDAFELSSMGIRVDADTLKHQLALTGDEDRLELEWHQALLRGEMPQTIGGGIGQSRL
TMLLLQLPHIGQVQCGVWPAAVRESVPSLL
References
External Links:
ResourceLink
Uniprot ID:P00963
Uniprot Name:ASNA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742336
PDB ID:12AS
Ecogene ID:EG10091
Ecocyc:EG10091
ColiBase:b3744
Kegg Gene:b3744
EchoBASE ID:EB0089
CCDB:ASNA_ECOLI
BacMap:16131612
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Buhk, H. J., Messer, W. (1983). "The replication origin region of Escherichia coli: nucleotide sequence and functional units." Gene 24:265-279. Pubmed: 6357950
  • Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Hirota, Y., Yasuda, S., Yamada, M., Nishimura, A., Sugimoto, K., Sugisaki, H., Oka, A., Takanami, M. (1979). "Structural and functional properties of the Escherichia coli origin of DNA replication." Cold Spring Harb Symp Quant Biol 43 Pt 1:129-138. Pubmed: 383377
  • Nakamura, M., Yamada, M., Hirota, Y., Sugimoto, K., Oka, A., Takanami, M. (1981). "Nucleotide sequence of the asnA gene coding for asparagine synthetase of E. coli K-12." Nucleic Acids Res 9:4669-4676. Pubmed: 6117826
  • Nakatsu, T., Kato, H., Oda, J. (1998). "Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase." Nat Struct Biol 5:15-19. Pubmed: 9437423
  • Sugiyama, A., Kato, H., Nishioka, T., Oda, J. (1992). "Overexpression and purification of asparagine synthetase from Escherichia coli." Biosci Biotechnol Biochem 56:376-379. Pubmed: 1369484