K6UCV4 · ADA_PLACD
- ProteinAdenosine deaminase
- GeneADA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids363 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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 (Probable)
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 (Probable)
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 | |
---|---|---|---|---|---|---|
87 μM | adenosine | 8 | ||||
8.7 μM | 5'-methylthioadenosine (MTA) | 8 |
kcat is 5.3 sec-1 with adenosine as substrate (PubMed:19728741).
kcat is 0.31 sec-1 with 5'-methylthioadenosine as substrate (PubMed:19728741).
kcat is 0.31 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Plasmodium)
Accessions
- Primary accessionK6UCV4
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000451868 | 1-363 | Adenosine deaminase | |||
Sequence: MNILQEPIDFLKKDEIKNIDLSQMSKKERYKIWKRIPKCELHCHLDLCFSADFFLSCIRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIRVADIFHDYEVIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKYKLDIELIHQAIVKGIKEVVELLDHKIHVALMCIGDTGHEAANIKASADFCLKHRADFVGFDHGGHEVDLKQYKEIFDYVRESGIPLSVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVSESQELIDMVKEKNILLEVCPISNVLLKNAKSMDTHPIRQLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLEDFMKMNEWALEKSFMDSNIKDKVKNLYF |
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)41,956
- Last updated2013-01-09 v1
- ChecksumE645736A256BD07F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DF157098 EMBL· GenBank· DDBJ | GAB65506.1 EMBL· GenBank· DDBJ | Genomic DNA |