Summary: Aspartate-ammonia ligase
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Aspartate-ammonia ligase Provide feedback
No Pfam abstract.
Internal database links
| SCOOP: | tRNA-synt_2 |
External database links
| SCOP: | 12as |
This tab holds annotation information from the InterPro database.
InterPro entry IPR004618
Aspartate--ammonia ligase (asparagine synthetase) EC catalyses the conversion of L-aspartate to L-asparagine in the presence of ATP and ammonia. This family represents one of the two non-homologous forms of aspartate--ammonia ligase found in Escherichia coli. This type is also found in Haemophilus influenzae, Treponema pallidum and Lactobacillus delbrueckii, but appears to have a very limited distribution. The fact that the protein from the H. influenzae is more than 70% identical to that from the spirochete T. pallidum, but less than 65% identical to that from the closely related E. coli, strongly suggests lateral transfer.
AsnA is a homodimeric enzyme which is structurally similiar to the catalytic core domain of class II aminoacyl-tRNA synthetases. Ammonia-dependent AsnA is not homologous to the glutamine-dependent asparagine synthetase AsnB [PUBMED:1346128].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | cytoplasm (GO:0005737) |
| Molecular function | aspartate-ammonia ligase activity (GO:0004071) |
| Biological process | asparagine biosynthetic process (GO:0006529) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan tRNA_synt_II (CL0040), which has the following description:
Aminoacyl-tRNA synthetases are key components of the protein translation machinery that catalyse two basic reactions. First, the activation of amino acids via the formation of aminoacyl adenylates and second, linking the activated amino acid to the cognate tRNAs. The aminoacyl-tRNA synthetases generate AMP as the second end product of this reaction, which differentiates them from the majority of ATP-dependent enzymes that produce ADP. In addition, there is a specific aminoacyl-tRNA synthetases for each of the 20 amino acids and there are two structurally distinct classes of aminoacyl-tRNA synthetases, each encompassing 10 different specificities. The two classes have alternative modes of aminoacylation: class I aminoacylate the 2'OH of the cognate tRNA; class II aminoacylate 3'OH (with the exception of PheRS). Each class contain a conserved core domain that is involved in ATP binding and hydrolysis and combines with additional domains that determine the specificity of interactions with the cognate amino acid and tRNA. The class II core domain consist of a mixed-beta sheet, similar to that found in the biotin synthetases, hence why this family has also been included in this clan. The core domain contains three modestly conserved motifs that are responsible for ATP binding. The class II aminoacyl-tRNA synthetases can contain additional nested domains, found inserted in the loops of the core domain [1] (and reference therein).
The clan contains the following 11 members:
AsnA BPL_LplA_LipB BPL_LplA_LipB_2 DUF366 tRNA-synt_2 tRNA-synt_2b tRNA-synt_2c tRNA-synt_2d tRNA-synt_2e tRNA-synt_His tRNA_synthFbetaAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (169) |
Full (1266) |
Representative proteomes | UniProt (4419) |
NCBI (5261) |
Meta (14) |
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| RP15 (378) |
RP35 (862) |
RP55 (1233) |
RP75 (1960) |
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| PP/heatmap | 1 | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (169) |
Full (1266) |
Representative proteomes | UniProt (4419) |
NCBI (5261) |
Meta (14) |
||||
|---|---|---|---|---|---|---|---|---|---|
| RP15 (378) |
RP35 (862) |
RP55 (1233) |
RP75 (1960) |
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| Raw Stockholm | |||||||||