O26742 · PUR1_METTH

Function

function

Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster per subunit.

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; N1-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site11Nucleophile
Binding site250[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site297Mg2+ (UniProtKB | ChEBI)
Binding site359Mg2+ (UniProtKB | ChEBI)
Binding site360Mg2+ (UniProtKB | ChEBI)
Binding site396[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site447[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site450[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionamidophosphoribosyltransferase activity
Molecular Functionmagnesium ion binding
Biological Process'de novo' IMP biosynthetic process
Biological Processglutamine metabolic process
Biological Processpurine nucleobase biosynthetic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Amidophosphoribosyltransferase
  • EC number
  • Short names
    ATase
  • Alternative names
    • Glutamine phosphoribosylpyrophosphate amidotransferase
      (GPATase
      )

Gene names

    • Name
      purF
    • Ordered locus names
      MTH_646

Organism names

Accessions

  • Primary accession
    O26742

Proteomes

PTM/Processing

Features

Showing features for propeptide, chain.

Type
IDPosition(s)Description
PropeptidePRO_00000292751-10
ChainPRO_000002927611-474Amidophosphoribosyltransferase

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-234Glutamine amidotransferase type-2

Sequence similarities

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    474
  • Mass (Da)
    52,660
  • Last updated
    1998-01-01 v1
  • MD5 Checksum
    CEE5D58006021A6F578425360600F0B9
MLGESEVRDKCGIVGIYSQDKKTGVASQIYYALYALQHRGQESAGISTFNGNDILTHRGMGLVCDVFNPEKLEELKGNVGIGHVRYSTTGESRIENSQPFWSEFQGGKIAIAHNGDIINSMELREELEEEGHNFVSTTDSEVICHLLSREYDEKPNMIYSIKRVSEQLVGSYSLVVLLNQDLYVVRDPVGIKPLAFARKGSTQIVASETVAFDVIGAEHVRDVQPGEILHLNRGKSYWVANAPNTRRAHCMFEYVYFARPDSVIDGRNVYRVRLNIGEALYREHPANADVVVPVPDSSIPAAIGYSRASGIPYGEGLIKNRYVGRTFIMPTQEERETAVKLKMNPIRSELEGKRIVLIDDSIVRGTTSRALIDIIRDAGAEEIHLRIGCPPIKSPCYYGIAMATKKELIASTRNVEEIRRIIGVDSLGYLSIESLVECIGIKKGFLCTGCLDGDYPTPLPSDISEYEAMRSCSR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE000666
EMBL· GenBank· DDBJ
AAB85151.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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