Top Level Name

  ⌊ Superfamily (extended) Glutaminase/Asparaginase

Family known
Total 100% <100% Family unknown
Functional domains 2672 0 0 2672
UniProtKB 21343 0 0 21343
GI 39445 0 0 39445
Structures 38
Reactions 0
Functional domains of this superfamily were last updated on Feb. 14, 2017
New functional domains were last added to this superfamily on April 30, 2013

Asparaginase, which is found in various plant, animal and bacterial cells, catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma. Glutaminase, a similar enzyme, catalyses the deaminination of glutamine to glutamic acid and an ammonium ion. Both enzymes are homotetramers: two threonine residues in the N-terminal half of the proteins are involved in the catalytic activity.

Jennings MP, Beacham IR

Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins

▸ Abstract

J Bacteriol 1990;172(3):1491-1498 | PubMed ID: 2407723

Minton NP, Bullman HM, Scawen MD, Atkinson T, Gilbert HJ

Nucleotide sequence of the Erwinia chrysanthemi NCPPB 1066 L-asparaginase gene

▸ Abstract

Gene 1986;46(1):25-35 | PubMed ID: 3026924

No notes.

Sequence Similarity Networks

Download a Sequence Similarity Network of this superfamily (XGMML format ).

Network downloads are XGMML files that are readable by program such as Cytoscape. In these networks, nodes represent proteins and edges represent pairwise similarities better than a given edge-score cutoff. The edge score is either a bit score for full networks or mean E values for a Repnet. Additionally, these networks contain several attributes with data from the SFLD.

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Full sequence similarity network is not available for this superfamily due to its size.
Repnet: 50% ID (22-Apr-2016)

List of files included in the download. A detailed list of included node attributes, their definitions, and their uses [revised: 1/24/2014].

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Multiple Sequence Alignment

View the alignment of a representative set of sequences of this superfamily using

Multiple Sequence Alignment

Align one or multiple sequences to the alignment of a representative set of sequences of this superfamily.
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Downloads

Data Type All (#) Known (#) Unknown (#)
Full length FASTA (2672) (0) (2672)
Complete annotation (.tsv) (2672) (0) (2672)
Annotation suitable for Excel ® (.tsv) (2672) (0) (2672)
Clear form

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To identify your sequence later, please make sure to provide a header line starting with '>' for each sequence. Empty headers are allowed, but a header line is always required.
Cutoff Value
The least significant edge-score at which pairwise similarities are included in the network. A bit score for the full network, or a mean E value for the Repnet.
XGMML format
Open in Cytoscape via:
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Download the annotation of all sequences as shown in the table below as a ͟Tab ͟Separated ͟Value (TSV) file. This file can be imported into a spreadsheet application.
Full length FASTA
Full length sequences in FASTA format.
Functional Domain FASTA
Sequences of the Functional Domain in FASTA format.
Complete annotation
Download complete annotation of sequences sets of this superfamily as a ͟Tab ͟Separated ͟Value (TSV) file. This file has all data but cell size can exceed the maximum supported by spreadsheet programs (such as Microsoft Excel ®).
Spreadsheet ready annotation
Annotation of sequences sets of this superfamily in a ͟Tab ͟Separated ͟Value (TSV) file. This file can be imported into a spreadsheet application. Cells which exceed the allowed spreadsheet maximum (32.5K) are preceded by the word "Truncated" and clipped short.
Total number of functional domains in this group.
Number of Functional Domains that have been manually or automatically been assigned to a family.
Number of Functional Domains that have not been assigned to a family.
Number of structures available from the PDB for members of this group.
Number of Functional Domains with 100% of Conserved Residues
Number of Functional Domains with less than 100% Conserved Residues