A0A1X0NMZ2 · A0A1X0NMZ2_9TRYP

  • Protein
    Adenylosuccinate synthetase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis.
Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.

Miscellaneous

Parasitic protozoa lack the de novo purine biosynthesis pathway and rely exclusively on the salvage pathway for their purine nucleotide requirements.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site97-103GTP (UniProtKB | ChEBI)
Active site98Proton acceptor
Binding site98Mg2+ (UniProtKB | ChEBI)
Binding site98-101IMP (UniProtKB | ChEBI)
Binding site125-128IMP (UniProtKB | ChEBI)
Binding site127Mg2+ (UniProtKB | ChEBI)
Binding site127-129GTP (UniProtKB | ChEBI)
Active site128Proton donor
Binding site212IMP (UniProtKB | ChEBI)
Binding site226IMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site338IMP (UniProtKB | ChEBI)
Binding site354IMP (UniProtKB | ChEBI)
Binding site478-484substrate
Binding site482IMP (UniProtKB | ChEBI)
Binding site484GTP (UniProtKB | ChEBI)
Binding site612-614GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionadenylosuccinate synthase activity
Molecular FunctionGTP binding
Molecular Functionmagnesium ion binding
Biological Process'de novo' AMP biosynthetic process
Biological ProcessIMP metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylosuccinate synthetase
  • EC number
  • Short names
    AMPSase
    ; AdSS
  • Alternative names
    • IMP--aspartate ligase

Gene names

    • ORF names
      TM35_000301140

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Edinburgh
  • Taxonomic lineage
    Eukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Trypanosoma

Accessions

  • Primary accession
    A0A1X0NMZ2

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias1-17Basic and acidic residues
Region1-39Disordered
Compositional bias19-39Polar residues

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    625
  • Mass (Da)
    69,340
  • Last updated
    2017-07-05 v1
  • MD5 Checksum
    2AE4B18BAD30B611A6B5CE613C2CDDC8
MTGCEMSREKNDRHADGNNKPSGAPQSPQRATESHNYTFPTSEAQRAVYDYLKKVKPIAELNQPTEVQTYTEASVKDVLHPLIESHNIIMVAGAFFGDEGKGKTVDAVSHHPGCTCIARVNSGENAGHTVYDDMGRKFVFNLAPSGLLTPGKRNYVGPECVMDPISFMEMEVSQLIAAKVSYQDRLFIGNVMIVTPYHKLLDLLASAPNSSTLKGMAPVHASKVTKRGIRLDHIFDDPEVMRRRLAKDMDTYFGFLKVKGLSDADVLRRCEEENSDGVQRVPQHVMDFAQASDKVEFLIQLYTERVKNNKEFPTRCDVTHELRSALARGEKVLLEGPQSYWLSNAREKFWESTTSADTTASGLLATAQFNFQRYNALVINVHKTPGSSRVGIGANPSSFVPQDYFSAQGIKTLKDLPNNMCVDFDSIQRLFFTKAFHADSKEFNGIWEPLEFEDASGKYNIGVAMAIASSRHHGECGAVTKKPRVCGFFDCVMHFEVTAVQGPYLSISALDRGDDYEKVGVTIAYIYYNPKKSVVNNNGRLYQNGDIIRAGDAVPSEAALHYCYPIVKLINGWKSTPIAASKRKEGDPLPRGVCEFIATVEHFTKAKVISIGNGPMGKDIIYIKQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-17Basic and acidic residues
Compositional bias19-39Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NBCO01000030
EMBL· GenBank· DDBJ
ORC86074.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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