P52201 · PUR8_SPICI

  • Protein
    Adenylosuccinate lyase
  • Gene
    purB
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate (ADS or N6-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate.

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 site4-5N6-(1,2-dicarboxyethyl)-AMP (UniProtKB | ChEBI)
Binding site67-69N6-(1,2-dicarboxyethyl)-AMP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
Molecular FunctionN6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
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 (ASase)

Gene names

    • Name
      purB

Organism names

  • Taxonomic identifier
  • Strain
    • R8A2HP
  • Taxonomic lineage
    Bacteria > Mycoplasmatota > Mollicutes > Entomoplasmatales > Spiroplasmataceae > Spiroplasma

Accessions

  • Primary accession
    P52201

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001378831-88Adenylosuccinate lyase

Interaction

Subunit

Homotetramer and homodimer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    88
  • Mass (Da)
    10,264
  • Last updated
    1996-10-01 v1
  • MD5 Checksum
    5E284AD97F2A953DB43B2C5E10FABD5B
MIERYFVTEIGKIWSDENKYNTWAKVELLVCEGWAQIGLIPPTDIEKIKTNLTVNLPRMLELEAETKHDVVAFTRMLSETLGPEKKWI

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue88

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L22971
EMBL· GenBank· DDBJ
AAA26587.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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