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.

A0A2S5VTK3 · A0A2S5VTK3_9MICO

  • Protein
    Phosphoribosylformylglycinamidine synthase subunit PurL
  • Gene
    purL
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
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; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide: step 1/2.

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site79
Binding site82ATP (UniProtKB | ChEBI)
Binding site126ATP (UniProtKB | ChEBI)
Binding site128Mg2+ 1 (UniProtKB | ChEBI)
Binding site129-132substrate
Active site130Proton acceptor
Binding site151substrate
Binding site152Mg2+ 2 (UniProtKB | ChEBI)
Binding site276substrate
Binding site304Mg2+ 2 (UniProtKB | ChEBI)
Binding site348-350substrate
Binding site536ATP (UniProtKB | ChEBI)
Binding site573ATP (UniProtKB | ChEBI)
Binding site574Mg2+ 1 (UniProtKB | ChEBI)
Binding site576substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functionphosphoribosylformylglycinamidine synthase activity
Biological Process'de novo' IMP biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoribosylformylglycinamidine synthase subunit PurL
  • EC number
  • Short names
    FGAM synthase
  • Alternative names
    • Formylglycinamide ribonucleotide amidotransferase subunit II
      (FGAR amidotransferase II
      ; FGAR-AT II
      )
    • Glutamine amidotransferase PurL
    • Phosphoribosylformylglycinamidine synthase subunit II

Gene names

    • Name
      purL
    • ORF names
      C5E16_08920

Organism names

  • Taxonomic identifier
  • Strain
    • AY1B3
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Clavibacter

Accessions

  • Primary accession
    A0A2S5VTK3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-22Disordered
Domain39-83Phosphoribosylformylglycinamidine synthase linker
Domain109-223PurM-like N-terminal
Domain237-391PurM-like C-terminal
Domain479-598PurM-like N-terminal
Domain612-752PurM-like C-terminal

Sequence similarities

Belongs to the FGAMS family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    789
  • Mass (Da)
    84,080
  • Last updated
    2018-07-18 v1
  • MD5 Checksum
    428B395E98A9F0711AA0CAE6E7BC1655
MSVHADPASVPTDPAGADARSARRHVADTVEMAERTPEKEQPYAALGLTEGEYLRIREILGRRPTSGELAMYSVMWSEHCSYKSSKKYLRQFGQKVSESMRKDLMVGMGENAGVVDVGEGWAVTFKIESHNHPSYIEPFQGAATGVGGIVRDIISMGARPVAVMDALRFGDIDDPDTARVVHGVVSGISFYGNCLGLPNIGGETYFDRVYQGNPLVNALAVGVLRHEDLHLANARGVGNKVVLFGARTGGDGIGGASILASDTFADGGPTKRPAVQVGDPFAEKVLIECCLELFREDLVEGIQDLGAAGISCATSELASNGDGGMHIRLEEVLLRDPSLTAEEILMSESQERMMAVVSPEKLEGFLAVVAKWDVETSVLGEVTDTGRLVIDHHGERIVDVEPRTVAVDGPVYDRPVAYPAWIDALQADSASRLARPTAPDDIRDQFLQLLGSPNLADASWITDQYDRYVMGNTALSFPDDAGMVRIDEESGLGFSVATDANGRFCQLDPYRGAQLALAEAYRNVAASGATPVAVSDCLNFGSPEDPEVMWQFSRTVEGLADGCLELEIPVTGGNVSLYNQTGTQAIHPTPVVGVLGVIDDVARRIPSGWQDEGDNIYLLGVTREELDGSAWAGTVHDHLGGVPPVVDLAAERDLASLIAAGGTQSLIASAHDLSDGGLGQALAESVMRFGVGARVWLDGIVQRDGVDAATALFSESTGRMLVTVPREDDVKFQGLCEGRGYPVLRIGVTDAQAPGLELQGLFTLSVDELRGVHRATLPARFGTVVEARA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PSXY01000012
EMBL· GenBank· DDBJ
PPF67587.1
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