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The annotation and conditions in this rule are derived from the following entries: P12042 (PURL_BACSU), Q9X0X3 (PURL_THEMA), Q5SMH8 (PURL_THET8)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 32 - 32 aligns to "H" in entry Q9X0X3 (individually applies "")
    • Subsequence at position 35 - 35 aligns to "Y" in entry Q9X0X3 (individually applies "ATP")
    • Subsequence at position 68 - 68 aligns to "[KR]" in entry Q9X0X3 (individually applies "ATP")
    • Subsequence at position 70 - 70 aligns to "E" in entry Q9X0X3 (individually applies "Magnesium 1")
    • Subsequence at position 71 - 74 aligns to "S-H-N-H" in entry Q9X0X3 (individually applies "Substrate binding")
    • Subsequence at position 72 - 72 aligns to "H" in entry Q9X0X3 (individually applies "Proton acceptor")
    • Subsequence at position 93 - 93 aligns to "R" in entry Q9X0X3 (individually applies "Substrate")
    • Subsequence at position 94 - 94 aligns to "D" in entry Q9X0X3 (individually applies "Magnesium 2")
    • Subsequence at position 189 - 189 aligns to "R" in entry Q9X0X3 (individually applies "Substrate; via carbonyl oxygen")
    • Subsequence at position 208 - 208 aligns to "Q" in entry Q9X0X3 (individually applies "Substrate")
    • Subsequence at position 236 - 236 aligns to "D" in entry Q9X0X3 (individually applies "Magnesium 2")
    • Subsequence at position 280 - 282 aligns to "E-S-Q" in entry Q9X0X3 (individually applies "Substrate binding")
    • Subsequence at position 442 - 442 aligns to "[ND]" in entry Q9X0X3 (individually applies "ATP")
    • Subsequence at position 477 - 477 aligns to "G" in entry Q9X0X3 (individually applies "ATP; via amide nitrogen and carbonyl oxygen")
    • Subsequence at position 478 - 478 aligns to "N" in entry Q9X0X3 (individually applies "Magnesium 1")
    • Subsequence at position 480 - 480 aligns to "S" in entry Q9X0X3 (individually applies "Substrate")

... then these annotations are applied i

Protein namei

  • Recommended name:
    Phosphoribosylformylglycinamidine synthase subunit PurL (EC:6.3.5.3)
    Short name:
    FGAM synthase
    Alternative name(s):
    Phosphoribosylformylglycinamidine synthase subunit II
    Formylglycinamide ribonucleotide amidotransferase subunit II
    Short name:
    FGAR amidotransferase II
    Short name:
    FGAR-AT II
    Glutamine amidotransferase PurL

Gene namei

  • Name:purL

Pathwayi

  • Pathwayi: IMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide. This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sequence similaritiesi

Subunit structurei

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

Functioni

  • 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.

Catalytic activityi

  • ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate.

Subcellular locationi

Regioni

  • Substrate binding (to residues corresponding to positions 71 - 74)
  • Substrate binding (to residues corresponding to positions 280 - 282)

Binding sitei

  • ATP (to residues corresponding to position 35)
  • ATP (to residues corresponding to position 68)
  • Substrate (to residues corresponding to position 93)
  • Substrate; via carbonyl oxygen (to residues corresponding to position 189)
  • Substrate (to residues corresponding to position 208)
  • ATP (to residues corresponding to position 442)
  • ATP; via amide nitrogen and carbonyl oxygen (to residues corresponding to position 477)
  • Substrate (to residues corresponding to position 480)

Metal bindingi

  • Magnesium 1 (to residues corresponding to position 70)
  • Magnesium 2 (to residues corresponding to position 94)
  • Magnesium 2 (to residues corresponding to position 236)
  • Magnesium 1 (to residues corresponding to position 478)

Active sitei

  • (to residues corresponding to position 32)
  • Proton acceptor (to residues corresponding to position 72)

Keywordsi

GO (Gene Ontology) termsi

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