K6UCV4 · ADA_PLACD

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)

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
87 μMadenosine8
8.7 μM5'-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).

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
      PCYB_062380

Organism names

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

Accessions

  • Primary accession
    K6UCV4

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004518681-363Adenosine deaminase

Structure

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)
    41,956
  • Last updated
    2013-01-09 v1
  • Checksum
    E645736A256BD07F
MNILQEPIDFLKKDEIKNIDLSQMSKKERYKIWKRIPKCELHCHLDLCFSADFFLSCIRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIRVADIFHDYEVIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKYKLDIELIHQAIVKGIKEVVELLDHKIHVALMCIGDTGHEAANIKASADFCLKHRADFVGFDHGGHEVDLKQYKEIFDYVRESGIPLSVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVSESQELIDMVKEKNILLEVCPISNVLLKNAKSMDTHPIRQLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLEDFMKMNEWALEKSFMDSNIKDKVKNLYF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DF157098
EMBL· GenBank· DDBJ
GAB65506.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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