A5KE01 · ADA_PLAVS

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).

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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 μMadenosine8
9.5 μM5'-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).

Pathway

Purine metabolism; purine nucleoside salvage.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site42Zn2+ (UniProtKB | ChEBI); catalytic
Binding site44Zn2+ (UniProtKB | ChEBI); catalytic
Binding site44-46a purine D-ribonucleoside (UniProtKB | ChEBI)
Binding site172a purine D-ribonucleoside (UniProtKB | ChEBI)
Site172Important for substrate specificity for S-methyl-5'-thioadenosine
Binding site201a purine D-ribonucleoside (UniProtKB | ChEBI)
Binding site226Zn2+ (UniProtKB | ChEBI); catalytic
Binding site229a purine D-ribonucleoside (UniProtKB | ChEBI)
Binding site253a purine D-ribonucleoside (UniProtKB | ChEBI)
Binding site310a purine D-ribonucleoside (UniProtKB | ChEBI)
Binding site310Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Molecular Function2'-deoxyadenosine deaminase activity
Molecular Function5'-methylthioadenosine deaminase activity
Molecular Functionadenosine deaminase activity
Molecular Functionmetal ion binding
Biological Processpurine ribonucleoside monophosphate biosynthetic process
Biological Processpurine ribonucleoside salvage

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenosine deaminase
  • EC number
  • Alternative names
    • S-methyl-5'-thioadenosine deaminase
      (EC:3.5.4.31
      ) . EC:3.5.4.31 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      ADA
    • ORF names
      PVX_111245

Organism names

  • Taxonomic identifier
  • Strain
    • Salvador I
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Plasmodium)

Accessions

  • Primary accession
    A5KE01

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis172Loss of S-methyl-5'-thioadenosine deaminase activity. Slight decrease in adenosine deaminase activity.
Mutagenesis172Loss of S-methyl-5'-thioadenosine deaminase activity. Slight decrease in adenosine deaminase activity.
Mutagenesis172Loss of S-methyl-5'-thioadenosine deaminase activity. No effect on adenosine deaminase activity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004518651-363Adenosine deaminase

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region170-184Gating helix loop; regulates binding affinity for substrates and thus substrate selectivity

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    363
  • Mass (Da)
    41,871
  • Last updated
    2007-07-10 v1
  • Checksum
    951357683E2964C1
MNILQEPIDFLKKEELKNIDLSQMSKKERYKIWKRIPKCELHCHLDLCFSADFFVSCIRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIKVADIFHDYEVIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKYNLDIELIHQAIVKGIKEVVELLDHKIHVALMCIGDTGHEAANIKASADFCLKHKADFVGFDHGGHEVDLKEYKEIFDYVRESGVPLSVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVAESQELIDMVKEKNILLEVCPISNVLLKNAKSMDTHPIRQLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLEDFMKMNEWALEKSFMDSNIKDKIKNLYF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAKM01002769
EMBL· GenBank· DDBJ
EDL42450.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp