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A5KBL5 · A5KBL5_PLAVS

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.
Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site13AMP (UniProtKB | ChEBI)
Binding site14AMP (UniProtKB | ChEBI)
Binding site86AMP (UniProtKB | ChEBI)
Binding site87AMP (UniProtKB | ChEBI)
Binding site88AMP (UniProtKB | ChEBI)
Binding site122AMP (UniProtKB | ChEBI)
Binding site280Ca2+ (UniProtKB | ChEBI)
Binding site334AMP (UniProtKB | ChEBI)
Binding site339AMP (UniProtKB | ChEBI)
Binding site343AMP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
Molecular Functionmetal ion binding
Molecular FunctionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
Molecular Functionnucleotide binding
Biological Process'de novo' AMP biosynthetic process
Biological Process'de novo' IMP biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylosuccinate lyase
  • EC number
  • Short names
    ASL
  • Alternative names
    • Adenylosuccinase

Gene names

    • ORF names
      PVX_003765

Organism names

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

Accessions

  • Primary accession
    A5KBL5

Proteomes

Organism-specific databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain12-311Fumarate lyase N-terminal
Domain330-446Adenylosuccinate lyase PurB C-terminal

Sequence similarities

Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    464
  • Mass (Da)
    53,158
  • Last updated
    2007-07-10 v1
  • MD5 Checksum
    A776C800BECA680702151C87B3E07638
MEHLKNISPIDGRYKKACGELSAFFSEHALIKHRIIVEVRWLLFLNEEELFFEKVTDHSVEVLNQIATNITDSDIARVKAIEEETNHDVKAVEYFVKEKLKNSKREDLLKIKEYVHYLCTSEDINNVAYATCLKACLNDVVIPCLEKIMLKLKDLAVEYSHVPLLSRTHGQPASSTTFGKEMANFYARIHHHVGVIRRVKVCAKFNGAVGNFNAHKVASKDTDWVNTIGLFLKKHFNLTYSIYCTQIQDHDYICELCDGLARANGTLIDLCVDIWLYISNNLLKLKVKEKEVGSSTMPHKVNPIDFENAEGNLHIANAFFKLFSSKLPTSRLQRDLSDSTVLRNIGSSLAYCLIAYKSVLKGLNKIDIDRRNLEEELNQNWSTLAEPIQIVMKRHNYVDAYEELKQFTRGKVIDQKIMQEFIKTKCAFLPQDVVDQLLELTPATYTGYADYLAKNVERLSGERD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAKM01000018
EMBL· GenBank· DDBJ
EDL43265.1
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.
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