Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

The annotation and conditions in this rule are derived from the following entries: P32173 (MOBA_ECOLI)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 12 - 14 aligns to "[LFIVT]-x-G" in entry P32173 (individually applies "GTP")
    • Subsequence at position 25 - 25 aligns to "[KR]" in entry P32173 (individually applies "GTP")
    • Subsequence at position 53 - 53 aligns to "[NRHK]" in entry P32173 (individually applies "GTP")
    • Subsequence at position 71 - 71 aligns to "D" in entry P32173 (individually applies "GTP")
    • Subsequence at position 101 - 101 aligns to "D" in entry P32173 (individually applies "GTP")
    • Subsequence at position 101 - 101 aligns to "D" in entry P32173 (individually applies "Magnesium")

... then these annotations are applied i

Protein namesi

  • Recommended name:
    Molybdenum cofactor guanylyltransferase (EC:2.7.7.77)
    Short name:
    MoCo guanylyltransferase
    Alternative name(s):
    Molybdopterin-guanine dinucleotide synthase
    Short name:
    MGD synthase
    Mo-MPT guanylyltransferase
    GTP:molybdopterin guanylyltransferase
    Molybdopterin guanylyltransferase
  • Recommended name:
    Probable molybdenum cofactor guanylyltransferase (EC:2.7.7.77)
    Short name:
    MoCo guanylyltransferase
    Alternative name(s):
    GTP:molybdopterin guanylyltransferase
    Molybdopterin-guanine dinucleotide synthase
    Short name:
    MGD synthase
    Mo-MPT guanylyltransferase
    Molybdopterin guanylyltransferase

Gene namei

  • Name:mobA

Subunit structurei

  • Monomer.

Functioni

  • Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.

Domaini

  • The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.

Subcellular locationi

Sequence similaritiesi

Cofactori

Catalytic activityi

  • GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor.

Binding sitei

  • GTP (to residues corresponding to position 25)
  • GTP (to residues corresponding to position 53)
  • GTP (to residues corresponding to position 71)
  • GTP (to residues corresponding to position 101)

Nucleotide bindingi

  • GTP (to residues corresponding to positions 12 - 14)

Metal bindingi

  • Magnesium (to residues corresponding to position 101)

Keywordsi

GO (Gene Ontology) termsi

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health