Summary: Asparagine synthase
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Asparagine synthase Provide feedback
This family is always found associated with PF00310. Members of this family catalyse the conversion of aspartate to asparagine.
Internal database links
| Similarity to PfamA using HHSearch: | NAD_synthase PAPS_reduct ThiI tRNA_Me_trans ATP_bind_3 QueC |
External database links
| PANDIT: | PF00733 |
| Pseudofam: | PF00733 |
| SCOP: | 1ct9 |
| SYSTERS: | Asn_synthase |
This tab holds annotation information from the InterPro database.
InterPro entry IPR001962
This domain is always found associated with (INTERPRO). Family members that contain this domain catalyse the conversion of aspartate to asparagine. Asparagine synthetase B (EC) catalyzes the assembly of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase [PUBMED:10587437].Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | asparagine synthase (glutamine-hydrolyzing) activity (GO:0004066) |
| 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 HUP (CL0039), which contains the following 26 members:
Arginosuc_synth Asn_synthase ATP-sulfurylase ATP_bind_3 ATP_bind_4 Citrate_ly_lig CTP_transf_2 DNA_photolyase ETF FAD_syn HIGH_NTase1 NAD_synthase Pantoate_ligase PAPS_reduct QueC ThiI tRNA-synt_1 tRNA-synt_1_2 tRNA-synt_1b tRNA-synt_1c tRNA-synt_1d tRNA-synt_1e tRNA-synt_1f tRNA-synt_1g tRNA_Me_trans UspAlignments
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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
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 (104) |
Full (5876) |
Representative proteomes | NCBI (12423) |
Meta (8100) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (735) |
RP35 (1406) |
RP55 (1834) |
RP75 (2130) |
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| Jalview | ||||||||
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| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
Download options
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 (104) |
Full (5876) |
Representative proteomes | NCBI (12423) |
Meta (8100) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (735) |
RP35 (1406) |
RP55 (1834) |
RP75 (2130) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_443 (release 2.1) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Bateman A, Griffiths-Jones SR |
| Number in seed: | 104 |
| Number in full: | 5876 |
| Average length of the domain: | 248.10 aa |
| Average identity of full alignment: | 24 % |
| Average coverage of the sequence by the domain: | 44.92 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 255 | ||||||||||||
| Family (HMM) version: | 16 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
ShowThis visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
Tree controls
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Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Asn_synthase domain has been found. There are 38 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence