F7BUU3 · F7BUU3_MONDO

Function

function

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

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 site59-65GTP (UniProtKB | ChEBI)
Active site60Proton acceptor
Binding site60Mg2+ (UniProtKB | ChEBI)
Binding site60substrate
Binding site60-63IMP (UniProtKB | ChEBI)
Binding site85-88IMP (UniProtKB | ChEBI)
Binding site87Mg2+ (UniProtKB | ChEBI)
Binding site87-89GTP (UniProtKB | ChEBI)
Active site88Proton donor
Binding site182IMP (UniProtKB | ChEBI)
Active site193
Binding site196IMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site275IMP (UniProtKB | ChEBI)
Binding site290IMP (UniProtKB | ChEBI)
Binding site350-356substrate
Binding site354IMP (UniProtKB | ChEBI)
Binding site356GTP (UniProtKB | ChEBI)
Binding site382-384GTP (UniProtKB | ChEBI)
Binding site464-467GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmitochondrion
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 isozyme 2
  • EC number
  • Short names
    AMPSase 2
    ; AdSS 2
  • Alternative names
    • Adenylosuccinate synthetase, acidic isozyme
    • Adenylosuccinate synthetase, liver isozyme
      (L-type adenylosuccinate synthetase
      )
    • IMP--aspartate ligase 2

Gene names

    • Name
      ADSS
    • Synonyms
      ADSS2

Organism names

Accessions

  • Primary accession
    F7BUU3

Proteomes

Subcellular Location

Keywords

Expression

Gene expression databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    476
  • Mass (Da)
    52,096
  • Last updated
    2019-12-11 v3
  • Checksum
    80CBDD022556AB35
NWVWQAPGCKNTQILTAARAMSLAEAGLAVASVPNGECGSSLARSGGNRVTVVLGAQWGDEGKGKVVDLLAQDADIVCRCQGGNNAGHTVVVDSVEYDFHLLPSGIINPNVTAFIGNGVVIHLPGLFEEAEKNVQKGKGLEGWEKRLIISDRAHIVFDFHQAADGIQEQQRQEQAGKNLGTTKKGIGPVYSSKASRSGLRMCDLVSDFEGFSERFKVLANQYKSIYPTLEIDIEGELQKLKGYMERIKPMVRDGVYFLYEALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAYTTRVGIGAFPTEQNNEIGELLQTRGREFGVTTGRKRRCGWLDLVLLKYAHMINGFTALALTKLDILDVFTEIKVGVAYKLDGEIIPHFPANQEVLNKVEVQYKTLPGWNTDISNARTFKDLPVNAQNYVQFIQDELQIPVKWIGVGKSRESMIQLF

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A5F8G4H9A0A5F8G4H9_MONDOADSS456
A0A5F8H2W3A0A5F8H2W3_MONDOADSS445
A0A5F8GLQ3A0A5F8GLQ3_MONDOADSS447

Keywords

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