A1RQP5 · PURP_PYRIL

Function

function

Catalyzes the ATP- and formate-dependent formylation of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of folates.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 1 Mg2+ or Mn2+ ion per subunit.

Pathway

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site205-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (UniProtKB | ChEBI)
Binding site855-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (UniProtKB | ChEBI)
Binding site136-187ATP (UniProtKB | ChEBI)
Binding site209ATP (UniProtKB | ChEBI)
Binding site2295-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (UniProtKB | ChEBI)
Binding site268Mg2+ (UniProtKB | ChEBI)
Binding site281Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionligase activity, forming carbon-nitrogen bonds
Molecular Functionmagnesium ion binding
Biological Process'de novo' IMP biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase
  • EC number
  • Alternative names
    • 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate--formate ligase

Gene names

    • Name
      purP
    • Ordered locus names
      Pisl_0094

Organism names

Accessions

  • Primary accession
    A1RQP5

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003486341-3335-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain106-313ATP-grasp

Sequence similarities

Belongs to the phosphohexose mutase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    333
  • Mass (Da)
    37,993
  • Last updated
    2008-09-02 v2
  • Checksum
    D0FE1A2EA510D1BE
MSVLKRYDLEKLAVATVASHTALQILRGAKKYGFRTIAIAGRADVAEFYQQFNFIDEVWTVDFRNFVKAAEKLVEANAVFIPHGSYVEYVGWRQALEAPVPTLGCRELIKWEADQYKKMELLQRGGIPTSRVYKTPEEVDRPVIVKLFGAKGGRGYFLARDREELRRRLAGLSDYIIQEYVFGVPAYYHYFSSPVYGRVEVFGADIRYESNVDGRTFGWVEPTFVVVGNLPLVLRESLLPTIWKYGVQFAKAVEEVVGCRLAGPYCLESIIRDDMSISVFEFSGRIVAGTNIYMGYGSPYSVLYFDRPMDMGERIAHEIREAARRGRLEDLFT

Sequence caution

The sequence ABL87277.1 differs from that shown. Reason: Erroneous initiation

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000504
EMBL· GenBank· DDBJ
ABL87277.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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