A5KE01 · ADA_PLAVS
- ProteinAdenosine deaminase
- GeneADA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids363 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the hydrolytic deamination of adenosine to produce inosine (PubMed:19728741).
Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI) (PubMed:19728741).
Plays an essential role in the purine salvage pathway which allows the parasite to use host cell purines for the synthesis of nucleic acids (PubMed:19728741).
Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI) (PubMed:19728741).
Plays an essential role in the purine salvage pathway which allows the parasite to use host cell purines for the synthesis of nucleic acids (PubMed:19728741).
Catalytic activity
- adenosine + H+ + H2O = inosine + NH4+
Cofactor
Note: Binds 1 zinc ion per subunit.
Activity regulation
Inhibited by coformycin and methylthiocoformycin (MT-coformycin).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
60 μM | adenosine | 8 | ||||
9.5 μM | 5'-methylthioadenosine (MTA) | 8 |
kcat is 1.8 sec-1 with adenosine as substrate (PubMed:19728741).
kcat is 0.13 sec-1 with 5'-methylthioadenosine as substrate (PubMed:19728741).
kcat is 0.13 sec-1 with 5'-methylthioadenosine as substrate (PubMed:19728741).
Pathway
Purine metabolism; purine nucleoside salvage.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 42 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 44 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 44-46 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: HLD | ||||||
Binding site | 172 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 172 | Important for substrate specificity for S-methyl-5'-thioadenosine | ||||
Sequence: D | ||||||
Binding site | 201 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 226 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 229 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 253 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 310 | a purine D-ribonucleoside (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 310 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 2'-deoxyadenosine deaminase activity | |
Molecular Function | 5'-methylthioadenosine deaminase activity | |
Molecular Function | adenosine deaminase activity | |
Molecular Function | metal ion binding | |
Biological Process | purine ribonucleoside monophosphate biosynthetic process | |
Biological Process | purine ribonucleoside salvage |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenosine deaminase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Plasmodium)
Accessions
- Primary accessionA5KE01
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 172 | Loss of S-methyl-5'-thioadenosine deaminase activity. Slight decrease in adenosine deaminase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 172 | Loss of S-methyl-5'-thioadenosine deaminase activity. Slight decrease in adenosine deaminase activity. | ||||
Sequence: D → E | ||||||
Mutagenesis | 172 | Loss of S-methyl-5'-thioadenosine deaminase activity. No effect on adenosine deaminase activity. | ||||
Sequence: Missing |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000451865 | 1-363 | Adenosine deaminase | |||
Sequence: MNILQEPIDFLKKEELKNIDLSQMSKKERYKIWKRIPKCELHCHLDLCFSADFFVSCIRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIKVADIFHDYEVIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKYNLDIELIHQAIVKGIKEVVELLDHKIHVALMCIGDTGHEAANIKASADFCLKHKADFVGFDHGGHEVDLKEYKEIFDYVRESGVPLSVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVAESQELIDMVKEKNILLEVCPISNVLLKNAKSMDTHPIRQLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLEDFMKMNEWALEKSFMDSNIKDKIKNLYF |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 170-184 | Gating helix loop; regulates binding affinity for substrates and thus substrate selectivity | ||||
Sequence: IGDTGHEAANIKASA |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length363
- Mass (Da)41,871
- Last updated2007-07-10 v1
- Checksum951357683E2964C1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAKM01002769 EMBL· GenBank· DDBJ | EDL42450.1 EMBL· GenBank· DDBJ | Genomic DNA |