PROSITE documentation PDOC00419Adenosine and AMP deaminase signature (original) (raw)
Description
Adenosine deaminase (EC 3.5.4.4) catalyzes the hydrolytic deamination of adenosine into inosine. AMP deaminase (EC 3.5.4.6) catalyzes the hydrolytic deamination of AMP into IMP. It has been shown [1] that these two types of enzymes share three regions of sequence similarities; these regions are centered on residues which are proposed to play an important role in the catalytic mechanism of these two enzymes. We have selected one of these regions, it contains two conserved aspartic acid residues that are potential active site residues.
Last update:
May 2004 / Text revised.
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Technical section
PROSITE method (with tools and information) covered by this documentation:
A_DEAMINASE, PS00485; Adenosine and AMP deaminase signature (PATTERN)
- Consensus pattern:
[SA]-[LIVM]-[NGS]-[STA]-D-D-P
The 2 D's may be active site residues - Sequences in UniProtKB/Swiss-Prot known to belong to this class: 189
- Other sequence(s) in UniProtKB/Swiss-Prot detected by PS00485:
21 false positives. - Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
Clustal format, color, condensed view / Clustal format, color / Clustal format, plain text / Fasta format - Retrieve the sequence logo from the alignment
- Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00485
- Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00485
- Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS00485
- View ligand binding statistics of PS00485
- Matching PDB structures: 1A4L 1A4M 1ADD 1KRM ... [ALL]
Reference
| 1 | Authors | Chang Z.Y. Nygaard P. Chinault A.C. Kellems R.E. |
|---|---|---|
| Title | Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: implications for catalytic function. | |
| Source | Biochemistry 30:2273-2280(1991). | |
| PubMed ID | 1998686 |
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