Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A430FPN8 · A0A430FPN8_9BIFI

  • Protein
    Formate-dependent phosphoribosylglycinamide formyltransferase
  • Gene
    purT
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.

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; IMP biosynthesis via de novo pathway; N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide from N1-(5-phospho-D-ribosyl)glycinamide (formate route): step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site51-52N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI)
Binding site111N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI)
Binding site143ATP (UniProtKB | ChEBI)
Binding site184ATP (UniProtKB | ChEBI)
Binding site189-194ATP (UniProtKB | ChEBI)
Binding site228-231ATP (UniProtKB | ChEBI)
Binding site236ATP (UniProtKB | ChEBI)
Binding site309Mg2+ (UniProtKB | ChEBI)
Binding site322Mg2+ (UniProtKB | ChEBI)
Binding site329N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI)
Binding site404N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI)
Binding site411-412N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionligase activity
Molecular Functionmagnesium ion binding
Molecular Functionphosphoribosylglycinamide formyltransferase 2 activity
Molecular Functionphosphoribosylglycinamide formyltransferase activity
Biological Process'de novo' IMP biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Formate-dependent phosphoribosylglycinamide formyltransferase
  • EC number
  • Alternative names
    • 5'-phosphoribosylglycinamide transformylase 2
    • Formate-dependent GAR transformylase
    • GAR transformylase 2
      (GART 2
      )
    • Non-folate glycinamide ribonucleotide transformylase
    • Phosphoribosylglycinamide formyltransferase 2

Gene names

    • Name
      purT
    • ORF names
      D2E26_0853

Organism names

  • Taxonomic identifier
  • Strain
    • 2036B
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A430FPN8

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-23Disordered
Domain148-351ATP-grasp

Sequence similarities

Belongs to the PurK/PurT family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    442
  • Mass (Da)
    47,124
  • Last updated
    2019-05-08 v1
  • MD5 Checksum
    13D8F478E05E3F193B173E4BBA428142
MTESTRHQIEPQTGPNTVSPTEQNVGFKANRTVGAPLGTHATRVLLLGSGELGKEVTIALQRLGVYVVAVDSYTGAPAHQVAHRNMVVDMANASQLRSLIAEINPDIIVPEIEAIATSELSAAAERGIQVVPSARVAQICMDREQLRTLAAQDLGLPTTPYEFAGTLDELKAAAKRIGFPCVVKPVMSSSGHGQSVVREAEQIEAAWREAQVGRRAAGEGDTSRVIVEKLVDLAAELTMLTVASSAGIVTCEPIGQRQEHGDYRESWQPADTQSAVLEEARRLAMQVVQGLVAVSQEHGEHGWGVYGVELFVLGDGTVLFNEVSPRPHDTGMVTMMSQRLSEFDLHARAILGLPITADHVALQIPPHTAAASHAIVVEGRGQALFNNLDVALSAANTDLRIFAKPEVNGHRRMAVALATGANSDEARVSAAQVVQSLDIEVV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QXGM01000002
EMBL· GenBank· DDBJ
RSX54799.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
Help